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  • 1.
    Andersson, Michael R.
    et al.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Samyn, Dieter R.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Persson, Bengt L.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Mutational analysis of conserved glutamic acids of Pho89, a Saccharomyces cerevisiae high-affinity inorganic phosphate:Na+ symporter2012In: Biologia (Bratislava), ISSN 0006-3088, E-ISSN 1336-9563, Vol. 67, no 6, p. 1056-1061Article in journal (Refereed)
    Abstract [en]

    In Saccharomyces cerevisiae, the high-affinity phosphate transport system comprises the Pho84 and Pho89 permeases. The Pho89 permease catalyzes import of inorganic phosphate in a symport manner by utilizing Na+ ions as co-solute. We have addressed the functional importance of two glutamic acid residues at positions 55 and 491. Both residues are highly conserved amongst members of the inorganic phosphate transporter (PiT) family, which might be an indication of functional importance. Moreover, both residues have been shown to be of critical importance in the hPit2 transporter. We have created site-directed mutations of both E55 and E491 to lysine and glutamine. We observed that in all four cases there is a dramatic impact on the transport activity, and thus it seems that they indeed are of functional importance. Following these observations, we addressed the membrane topology of this protein by using several prediction programs. TOPCONS predicts a 7-5 transmembrane segment organization, which is the most concise topology as compared to the hPiT2 transporter. By understanding the functionality of these residues, we are able to correlate the Pho89 topology to that of the hPiT2, and can now further analyze residues which might play a role in the transport activity.

  • 2.
    Basheer, Shabana
    et al.
    Central Food Technology Research Institute.
    Samyn, Dieter R.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Hedström, Martin
    Lund university.
    Thakur, Munna Singh
    Central Food Technology Research Institute.
    Persson, Bengt L.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Mattiasson, Bo
    Lund university.
    A membrane protein based biosensor: Use of a phosphate - H+ symporter membrane protein (Pho84) in the sensing of phosphate ions.2011In: Biosensors & bioelectronics, ISSN 0956-5663, E-ISSN 1873-4235, Vol. 27, no 1, p. 58-63Article in journal (Refereed)
    Abstract [en]

    A label free biosensor for direct detection of inorganic phosphate based on potential-step capacitance measurements has been developed. The high-affinity Pho84 plasma membrane phosphate/proton symporter of Saccharomyces cerevisiae was used as a sensing element. Heterologously expressed and purified Pho84 protein was immobilized on a self-assembled monolayer (SAM) on a capacitance electrode. Changes in capacitance were recorded upon exposure to phosphate compared to the control substance, phosphate analogue methylphosphonate. Hence, even without the explicit use of lipid membranes, the Pho84 membrane protein could retain its capacity of selective substrate binding, with a phosphate detection limit in the range of the apparent in vivo K(m). A linear increase in capacitance was monitored in the phosphate concentration range of 5-25 mu M. The analytical response of the capacitive biosensor is in agreement with that the transporter undergoes significant conformational changes upon exposure to inorganic phosphate, while exposure to the analogue only causes minor responses.

  • 3. Berhe, A
    et al.
    Fristedt, U
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Expression and purification of the high-affinity phosphate transporter of Saccharomyces cerevisiae1995In: European journal of biochemistry, Vol. 227, p. 566-572Article in journal (Refereed)
  • 4. Berhe, A
    et al.
    Zvyagilskaya, Renata
    Lagerstedt, J O
    Pratt, J R
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Properties of the Cysteine-less Pho84 Phosphate Transporter of Saccharomyces cerevisiae2001In: Biochemical and biophysical research communications, Vol. 287, p. 837-842Article in journal (Refereed)
  • 5. Braun, P
    et al.
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Kaback, H R
    von Heijne, G
    Alanine insertion scanning mutagenesis of lactose permease transmembrane helices1997In: Journal of biological chemistry, Vol. 272, p. 29566-29571Article in journal (Refereed)
  • 6. Carlenor, E
    et al.
    Persson, Bengt L.
    Department of Biochemistry, Arrhenius Laboratory, University of Stockholm.
    Glaser, E
    Andersson, B
    Rydström, J
    On the presence of a nicotinamide nucleotide transhydrogenase in mitochondria from potato tuber1988In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 88, p. 303-308Article in journal (Refereed)
    Abstract [en]

    Mitochondria isolated from potato (Solanum tuberosum L.) tuber wereinvestigated for the presence of a nicotinamide nucleotide transhydrogenaseactivity. Submitochondrial particles derived from these mitochondriaby sonication catalyzed a reduction of NAD' or 3-acetylpyridine-NAD'by NADPH, which showed a maximum of about 50 to 150 nanomoles/minute. milligram protein at pH 5 to 6. The Km values for 3-acetylpyridine-NAD' and NADPH were about 24 and 55 micromolar, respectively.Intact mitochondria showed a negligible activity in the absence of detergents.However, in the presence of detergents the specific activity approachedabout 30% of that seen with submitochondrial particles. Thepotato mitochondria transhydrogenase activity was sensitive to trypsinand phenylarsine oxide, both agents that are known to inhibit the mammaliantranshydrogenase. Antibodies raised against rat liver transhydrogenasecrossreacted with two peptides in potato tuber mitochondrialmembranes with a molecular mass of 100 to 115 kilodaltons. Theobserved transhydrogenase activities may be due to an unspecific activityof dehydrogenases and/or to a genuine transhydrogenase. The activitycontributions by NADH dehydrogenases and transhydrogenase to thetotal transhydrogenase activity were investigated by determining theirrelative sensitivities to trypsin. It is concluded that, at high or neutralpH, the observed transhydrogenase activity in potato tuber submitochondrialparticles is due to the presence of a genuine and specific highmolecular weight transhydrogenase. At low pH an unspecific reaction ofan NADH dehydrogenase with NADPH contributes to the total transhydrogenaseactivity. 

  • 7. Clyne, N
    et al.
    Persson, Bengt L.
    Department of Biochemistry, University of Stockholm.
    Havu, N
    Hultman, E
    Lins, L-E
    Pehrsson, S K
    Rydström, J
    Wibom, R
    The intracellular distribution of cobalt in exposed and unexposed rat myocardium1990In: Scandinavian Journal of Clinical and Laboratory Investigation, ISSN 0036-5513, E-ISSN 1502-7686, Vol. 50, no 6, p. 605-609Article in journal (Refereed)
    Abstract [en]

    The intracellular distribution of cobalt was analysed in the myocardium of exposed and unexposed rats. The exposed rats were given a dietary cobalt supplementation of 40 mg CoS04-7 H20/kg body weight for 8 weeks. The mitochondrial fraction showed the greatest relative increase in cobalt: 0.09 ng/mg protein in the unexposed rats to 8.43 ng/mg protein in the exposed rats. In the exposed rats the submitochondrial particles had the highest levels of cobalt: 19.43 ng/mg protein, followed by the sarcoplasmatic reticulum: 12.3 ng/mg protein. The microsomal 44 000g supernatant also showed an increase, although the levels remained low (0.51 ng/mg protein in the exposed animals). Apparently the calcium-storing organelles had the highest levels of cobalt. This could affect calcium flux in myocardial cells and, secondarily, tension development in cardiac muscle.

  • 8. Clyne, N
    et al.
    Wibom, R
    Havu, N
    Hultman, E
    Lins, L-E
    Pehrsson, S K
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Rydström, J
    The effect of cobalt on mitochondrial ATP production and cellular morphology in the rat myocardium and skeletal muscle1990In: Scandinavian Journal of Clinical and Laboratory Investigation, ISSN 0036-5513, E-ISSN 1502-7686, Vol. 50, p. 153-159Article in journal (Refereed)
  • 9. Consler, T G
    et al.
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Jung, H
    Zen, K
    Jung, K
    Privé, G G
    Verner, G E
    Kaback, H R
    Properties and purification of an active biotinylated lactose permease from Escherichia coli1993In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 90, p. 6934-6938Article in journal (Refereed)
  • 10. Daram, P
    et al.
    Brunner, S
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Amrhein, N
    Bucher, M
    Functional Analysis and Cell-Specific Expression of a Phosphate Transporter from Tomato1998In: Planta, Vol. 206, p. 225-233Article in journal (Refereed)
  • 11. Eytan, G D
    et al.
    Persson, Bengt L.
    UNIV STOCKHOLM, ARRHENIUS LAB, DEPT BIOCHEM.
    Ekebacke, A
    Rydström, J
    Energy-linked nicotinamide-nucleotide transhydrogenase. Characterization of reconstituted ATP-driven transhydrogenase from beef heart mitochondria.1987In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 262, p. 5008-5014Article in journal (Refereed)
    Abstract [en]

    The interaction between pure transhydrogenase and ATPase (Complex V) from beef heart mitochondria was investigated with transhydrogenase-ATPase vesicles in which the two proteins were co-reconstituted by dialysis or dilution procedures. In addition to phosphatidylcholine and phosphatidylethanolamine, reconstitution required phosphatidylserine and lysophosphatidylcholine. Transhydrogenase-ATPase vesicles catalyzed a 20-30-fold stimulation of the reduction of NADP+ or thio-NADP+ by NADH and a 70-fold shift of the apparent equilibrium expressed as the nicotinamide nucleotide ratio [NADPH][NAD+]/[NADP+][NADH]. In both of these respects, the transhydrogenase-ATPase vesicles were severalfold more efficient than beef heart submitochondrial particles. By measuring the ATP-driven transhydrogenase and the oligomycin-sensitive ATPase activities simultaneously and under the same conditions at low ATP concentrations, i.e. below 15 microM, the ATP-driven transhydrogenase/oligomycin-sensitive ATPase activity ratio was found to be about 3. This value is consistent with the stoichiometries of three protons translocated per ATP hydrolyzed and one proton translocated per NADPH formed and with a mechanism where the two enzymes interact through a delocalized proton-motive force. 

  • 12. Forsmark-André, P
    et al.
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Radi, R
    Dallner, G
    Ernster, L
    Oxidative modification of nicotinamide nucleotide transhydrogenase in submitochondrial particles. Effect of endogeneous ubiquinol1996In: Archives of biochemistry and biophysics, Vol. 336, p. 113-120Article in journal (Refereed)
  • 13. Frillingos, S
    et al.
    Sahin-Toth, M
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Kaback, H R
    Cysteine-scanning mutagenesis of putative helix VII in the lactose permease of Escherichia coli1994In: Biochemistry, Vol. 33, p. 8074-8081Article in journal (Refereed)
  • 14. Fristedt, U
    et al.
    Berhe, A
    Ensler, K
    Norling, B
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Characterization of isolated plasma membrane vesicles of Saccharomyces cerevisiae harboring the high-affinity phosphate transporter1996In: Archives of biochemistry and biophysics, Vol. 330, p. 133-141Article in journal (Refereed)
  • 15. Fristedt, U
    et al.
    Rydström, J
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Evidence for a nicotinamide nucleotide transhydrogenase in Klebsiella pneumoniae1994In: Biochemical and biophysical research communication, Vol. 198, p. 928-932Article in journal (Refereed)
  • 16. Fristedt, U
    et al.
    van der Rest, M
    Poolman, B
    Konings, W N
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Studies of Cytochrome c Oxidase-Driven H+-Coupled Phosphate Transport Catalyzed by the Saccharomyces cerevisiae Pho84 Permease in Co-Reconstituted Vesicles1999In: Biochemistry, Vol. 38, p. 16010-16015Article in journal (Refereed)
  • 17. Fristedt, U
    et al.
    Weinander, R
    Martinsson, H-S
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Characterization of Purified and Unidirectionally Reconstituted Pho84 Phosphate Permease of Saccharomyces cerevisiae1999In: FEBS letters, Vol. 458, p. 1-5Article in journal (Refereed)
  • 18. Hu, P-S
    et al.
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Höög, J-O
    Jörnvall, H
    Hartog, A F
    Berden, J
    Holmberg, E
    Rydström, J
    Energy-linked transhydrogenase. Characterization of a nucleotide binding sequence in nicotinamide nucleotide transhydrogenase from beef heart1992In: Biochimica et biophysica acta, Vol. 1102, p. 19-29Article in journal (Refereed)
  • 19. Jackson, J B
    et al.
    Lever, T M
    Rydström, J
    Persson, Bengt L.
    Department of Biochemistry and Biotechnology, Royal Institute of Technology .
    Carlenor, E
    Proton-translocating transhydrogenase from photosynthetic bacteria1991In: Biochemical Society Transactions, ISSN 0300-5127, E-ISSN 1470-8752, Vol. 19, no 3, p. 573-575Article in journal (Refereed)
  • 20.
    Johri, Atul K.
    et al.
    Jawaharlal Nehru Univ, India.
    Oelmueller, Ralf
    Univ Jena, Germany.
    Dua, Meenakshi
    Jawaharlal Nehru Univ, India.
    Yadav, Vikas
    Jawaharlal Nehru Univ, India.
    Kumar, Manoj
    Jawaharlal Nehru Univ, India.
    Tuteja, Narendra
    Int Ctr Genet Engn & Biotechnol, India;Amity Univ, India.
    Varma, Ajit
    Amity Univ, India.
    Bonfante, Paola
    Univ Turin, Italy.
    Persson, Bengt L.
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Stroud, Robert M.
    Univ Calif San Francisco, USA.
    Fungal association and utilization of phosphate by plants: success, limitations, and future prospects2015In: Frontiers in Microbiology, ISSN 1664-302X, E-ISSN 1664-302X, Vol. 6, article id 984Article, review/survey (Refereed)
    Abstract [en]

    Phosphorus (P) is a major macronutrient for plant health and development. The available form of P is generally low in the rhizosphere even in fertile soils. A major proportion of applied phosphate (Pi) fertilizers in the soil become fixed into insoluble, unavailable forms, which restricts crop production throughout the world. Roots possess two distinct modes of P uptake from the soil, direct and indirect uptake. The direct uptake of P is facilitated by the plant's own Pi transporters while indirect uptake occurs via mycorrhizal symbiosis, where the host plant obtains P primarily from the fungal partner, while the fungus benefits from plant-derived reduced carbon. So far, only one Pi transporter has been characterized from the mycorrhizal fungus Glomus versiforme. As arbuscular mycorrhizal fungi cannot be cultured axenically, their Pi transporter network is difficult to exploite for large scale sustainable agriculture. Alternatively, the root-colonizing endophytic fungus Piriformospora indica can grow axenically and provides strong growth-promoting activity during its symbiosis with a broad spectrum of plants. P indica contains a high affinity Pi transporter (PiPT) involved in improving Pi nutrition levels in the host plant under P limiting conditions. As P indica can be manipulated genetically, it opens new vistas to be used in P deficient fields.

  • 21. Lagerstedt, J O
    et al.
    Kruckeberg, A L
    Berden, J
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Yeast phosphate transporting System: Regulated Trafficking of the Pho84 Phosphate Transporting Protein2000In: Molecular biology and physiology of water and solute transport: Proceedings of the 3rd International Conference on Molecular Biology and Physiology of Water and Solute transport, held July 1-4, 2000, in Gothenburg, Sweden / [ed] Stefan Hohmann & Søren Nielson, New York: Kluwer Academic Publishers, 2000, p. 405-414Chapter in book (Other academic)
  • 22. Lagerstedt, J O
    et al.
    Voss, J C
    Wieslander, Åke
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Structural modelling of dual-affinity purified Pho84 phosphate transporter2004In: FEBS letters, Vol. 578, p. 262-268Article in journal (Refereed)
  • 23.
    Lagerstedt, Jens
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Reeve, I
    Voss, J C
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Structure and function of the GTP binding protein Gtr1 and its role in phosphate transport in Saccharomyces cerevisiae2005In: Biochemistry, Vol. 44 (2), p. 511-517Article in journal (Refereed)
  • 24.
    Lagerstedt, Jens
    et al.
    Växjö University, Faculty of Mathematics/Science/Technology, Institutionen för biovetenskaper och processteknik.
    Zvyagilskaya, Renata
    Pratt, James
    Växjö University, Faculty of Mathematics/Science/Technology, Institutionen för biovetenskaper och processteknik.
    Pattison-Granberg, Johanna
    Växjö University, Faculty of Mathematics/Science/Technology, Institutionen för biovetenskaper och processteknik.
    Kruckeberg, A L
    Berden, J
    Persson, Bengt L.
    Växjö University, Faculty of Mathematics/Science/Technology, Institutionen för biovetenskaper och processteknik.
    Mutagenic and Functional Analysis of the C-terminus of Saccharomyces cerevisiae Pho84 Phosphate Transporter2002In: FEBS letters, Vol. 526, p. 31-37Article in journal (Refereed)
  • 25. Li, T
    et al.
    Krasne, S J
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Kaback, H R
    Diederich, F
    Carriers for nucleotide 5’-triphosphates. Liquid membrane and liposome transport1993In: Journal of organic chemistry, Vol. 58, p. 380-384Article in journal (Refereed)
  • 26.
    Lundh, Fredrik
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Mouillon, Jean-Marie
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Samyn, Dieter R.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Stadler, Kent
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Popova, Yulia
    Lagerstedt, Jens
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Thevelein, Johan
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Molecular mechanisms controlling phosphate-induced downregulation of the yeast Pho84 phosphate transporter2009In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 48, no 21, p. 4497-4505Article in journal (Refereed)
    Abstract [en]

    In Saccharomyces cerevisiae, phosphate uptake is mainly dependent on the proton-coupled Pho84 permease under phosphate-limited growth conditions. Phosphate addition causes Pho84-mediated activation of the protein kinase A (PKA) pathway as well as rapid internalization and vacuolar breakdown of Pho84. We show that Pho84 undergoes phosphate-induced phosphorylation and subsequent ubiquitination on amino acids located in the large middle intracellular loop prior to endocytosis. The attachment of ubiquitin is dependent on the ubiquitin conjugating enzymes Ubc2 and Ubc4. In addition, we show that the Pho84 endocytotic process is delayed in strains with reduced PKA activity. Our results suggest that Pho84-mediated activation of the PKA pathway is responsible for its own downregulation by phosphorylation, ubiquination, internalization, and vacuolar breakdown.

  • 27. Martinez, P
    et al.
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Identification and characterization of a derepressible Na+-coupled phosphate transporter in Saccharomyces cerevisiae1998In: Molecular and General Genetics, Vol. 258, p. 628-638Article in journal (Refereed)
  • 28. Martinez, P
    et al.
    Zvyagilskaya, Renata
    Allard, P
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Physiological Regulation of the Derepressible Phosphate Transporter, Pho84p, in Saccharomyces cerevisiae1998In: Journal of bacteriology, Vol. 180, p. 2253-2256Article in journal (Refereed)
  • 29.
    Momeni, Naghi
    et al.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Bergquist, Jonas
    Uppsala University.
    Brudin, Lars
    Kalmar County Hospital.
    Behnia, Fatemeh
    University of Social Welfare and Rehabilitation Sciences, Iran.
    Sivberg, Bengt
    Lund University.
    Joghataei, Mohammad
    Tehran Medical University, Iran.
    Persson, Bengt L.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    A novel blood-based biomarker for detection of autism spectrum disorders2012In: Translational Psychiatry, ISSN 2158-3188, E-ISSN 2158-3188, Vol. 2, article id e91Article in journal (Refereed)
    Abstract [en]

    Autism Spectrum Disorders (ASD) are classified as neurological developmental disorders. Several studies have been carried out to find a candidate biomarker linked to development of these disorders, but up to date no reliable biomarker is available. Mass spectrometry techniques have been used for protein profiling of blood plasma of children with such disorders in order to identify proteins/peptides which may be used as biomarkers for detection of the disorders. Three differentially expressed peptides with mass charged (m/z) values of 2,020 ± 1, 1,864 ± 1, and 1,978 ± 1 Da in heparin plasma of children with ASD which were significantly changed as compared to the peptide pattern of the non-ASD control group are reported here. This novel set of biomarkers allows for a reliable blood based diagnostic tool that may be used in diagnosis and potentially, in prognosis of ASD. 

  • 30.
    Momeni, Naghi
    et al.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Brudin, Lars
    Kalmar County Hospital.
    Behnia, Fatemeh
    University of Social Welfare and rehabilitation Sciences, Iran.
    Nordström, Berit
    Lund University.
    Yousefi-Oudarji, Ali
    Tehran University of Medical Sciences, Iran.
    Sivberg, Bengt
    Lund University.
    Joghataei, Mohammad
    Tehran University of Medical Sciences, Iran.
    Persson, Bengt L.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    High complement factor I activity in the plasma of children with autism spectrum disorders2012In: Autism Research and Treatment, ISSN 2090-1925, E-ISSN 2090-1933, article id 868576Article in journal (Refereed)
    Abstract [en]

    Autism spectrum disorders (ASDs) are neurodevelopmental and behavioural syndromes affecting social orientation, behaviour, and communication that can be classified as developmental disorders. ASD is also associated with immune system abnormality. Immune system abnormalities may be caused partly by complement system factor I deficiency. Complement factor I is a serine protease present in human plasma that is involved in the degradation of complement protein C3b, which is a major opsonin of the complement system. Deficiency in factor I activity is associated with an increased incidence of infections in humans. In this paper, we show that the mean level of factor I activity in the ASD group is significantly higher than in the control group of typically developed and healthy children, suggesting that high activity of complement factor I might have an impact on the development of ASD.

  • 31.
    Mouillon, Jean-Marie
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Inhibition of the protein kinase A alters the degradation of the high-affinity phosphate transporter Pho84 in Saccharomyces cerevisiae2005In: Current genetics, Vol. 48 (4), p. 226-234Article in journal (Refereed)
  • 32.
    Mouillon, Jean-Marie
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    New aspects on phosphate sensing and signalling in Saccharomyces cerevisiae2006In: FEMS yeast research, Vol. 6, no 6, p. 171-176Article in journal (Refereed)
  • 33. Ormö, M
    et al.
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Rydström, J
    Correlation between active form and dimeric structure of mitochondrial nicotinamide nucleotide transhydrogenase from beef heart1992In: Journal of bioenergetics and biomembranes, Vol. 24, p. 611-615Article in journal (Refereed)
  • 34. Pattison-Granberg, J
    et al.
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Regulation of Cation-Coupled High-Affinity Phosphate Uptake in the Yeast Saccharomyces cerevisiae2000In: Journal of bacteriology, Vol. 182, p. 5017-5019Article in journal (Refereed)
  • 35.
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    The PHO regulon2004In: Encyclopedia of biological chemistry: Vol. 3 N-R / [ed] William J. Lennarz and M. Daniel Lane, Oxford: Academic Press, 2004, 1, , p. 262-265p. 262-265Chapter in book (Other academic)
  • 36.
    Persson, Bengt L.
    et al.
    Department of Biochemistry, Arrhenius Laboratory, University of Stockholm.
    Ahnström, G
    Rydström, J
    Energy-linked nicotinamide nucleotide transhydrogenase. Hydrodynamic properties and active form of purified and membrane-bound mitochondrial transhydrogenase from beef heart1987In: Archives of Biochemistry and Biophysics, ISSN 0003-9861, E-ISSN 1096-0384, Vol. 259, no 2, p. 341-349Article in journal (Refereed)
    Abstract [en]

    The mitochondrial nicotinamide nucleotide transhydrogenase from beef heart was investigated with respect to minimal assembly of the purified enzyme and of the enzyme in the mitochondrial inner membrane. Studies of the hydrodynamic properties of the purified enzyme in the presence of 0.3% Triton X-100 allowed determination of the Stokes radius, sedimentation constant, partial specific volume, frictional ratio, and molecular weight. Under these conditions transhydrogenase existed as an inactive monomer, suggesting that monomerization may be accompanied by inactivation. Radiation inactivation was used to determine the functional molecular size of purified detergent-dispersed transhydrogenase and transhydrogenase in beef heart submitochondrial particles. Under these conditions the catalytic activity of both the purified and the membrane-bound enzyme was found to be catalyzed by a dimeric form of the enzyme. These results suggest for the first time that the minimal functional assembly of detergent-dispersed as well as membrane-bound transhydrogenase is a dimer, which is not functionally associated with, for example, complex I or ATPase. In addition, the results are consistent with the possibility that the two subunits of transhydrogenase are catalytically active in an alternating fashion according to a previously proposed half-of-the-sites reactivity model. 

  • 37.
    Persson, Bengt L.
    et al.
    Laboratory of Biochemistry, B.C.P. Jansen Institute, University of Amsterdam, Amsterdam The Netherlands.
    Berden, J
    Rydström, J
    van Dam, K
    ATP-driven transhydrogenase provides an example of delocalized chemiosmotic coupling in reconstituted vesicles and in submitochondrial particles1987In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 894, no 2, p. 239-251Article in journal (Refereed)
    Abstract [en]

    The mechanism of coupling between mitochondrial ATPase (EC 3.6.1.3) and nicotinamide nucleotide transhydrogenase (EC 1.6.1.1) was studied in reconstituted liposomes containing both purified enzymes and compared with their behavior in submitochondrial particles. In order to investigate the mode of coupling between the transhydrogenase and the ATPase by the double-inhibitor and inhibitor-uncoupler methods, suitable inhibitors of transhydrogenase and ATPase were selected. Phenylarsine oxide and A3′-O-(3-(N-(4-azido-2-nitrophenyl)amino)propionyl)-NAD+ were used as transhydrogenase inhibitors, whereas of the various ATPase inhibitors tested aurovertin was found to be the most convenient. The inhibition of the ATP-driven transhydrogenase activity was proportional to the inhibition of both the ATPase and the transhydrogenase. Inhibitor-uncoupler titrations showed an increased sensitivity of the coupled reaction towards carbonyl cyanide p-trifluoromethoxyphenylhydrazone (FCCP) — an uncoupler that preferentially uncouples localized interactions, according to Herweijer et al. (Biochim. Biophys. Acta 849 (1986) 276–287) — when the primary pump was partially inhibited. However, when the secondary pump was partially inhibited the sensitivity towards FCCP remained unchanged. Similar results were obtained with submitochondrial particles. These results are in contrast to those obtained previously with the ATP-driven reverse electron flow. In addition, the amount of uncoupler required for uncoupling of the ATP-driven transhydrogenase was found to be similar to that required for the stimulation of the ATPase activity, both in reconstituted vesicles and in submitochondrial particles. Uncoupling of reversed electron flow to NAD+ required much less uncoupler. On the basis of these results, it is proposed that, in agreement with the chemiosmotic model, the interaction between ATPase and transhydrogenase in reconstituted vesicles as well as in submitochondrial particles occurs through the [...]. In contrast, the energy transfer between ATPase and NADH-ubiquinone oxidoreductase appears to occur via a more direct interaction, according to the above-mentioned results by Herweijer et al. 

  • 38.
    Persson, Bengt L.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Berhe, A
    Fristedt, U
    Martinez, P
    Pattison, J
    Petersson, J
    Weinander, R
    Phosphate permeases of Saccharomyces cerevisiae1998In: Biochimica et biophysica acta, Vol. 1365, p. 23-30Article in journal (Refereed)
  • 39.
    Persson, Bengt L.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Carenor, E
    Clyne, N
    Hultman, E
    Lins, L-E
    Pehrsson, S K
    Rydström, J
    Binding of cobalt to sarcoplasmatic reticulum proteins1992In: Scandinavian journal of clinical and laboratory investigation, Vol. 52 (2), p. 137-140Article in journal (Refereed)
  • 40.
    Persson, Bengt L.
    et al.
    the Department of Biochemistry, Arrhenius Laboratory, University of Stockholm.
    Enander, K
    the Department of Biochemistry, Arrhenius Laboratory, University of Stockholm.
    Tang, H-L
    Rydström, J
    the Department of Biochemistry, Arrhenius Laboratory, University of Stockholm.
    Energy-linked nicotinamide nucleotide transhydrogenase: Properties of proton-translocating mitochondrial transhydrogenase from beef heart purified by fast protein liquid chromatography1984In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 259, p. 8626-8632Article in journal (Refereed)
    Abstract [en]

    Mitochondrial nicotinamide nucleotide transhydrogenasefrom beef heart was purified by a novel procedureinvolving fast protein liquid chromatography andcharacterized with respect to molecular and catalyticproperties. The method is reproducible, gives highlypure transhydrogenase as judged by silver staining,and can be modified to produce large amounts of puretranshydrogenase protein suitable for e.g. sequencingand other protein chemical studies.Transhydrogenase purified by fast protein liquidchromatography is reconstitutively active and pumpsprotons as indicated by an extensive quenching of 9-aminoacridine fluorescence. Under conditions whichgenerate a proton gradient in the absence of a membranepotential the activity of reconstituted transhydrogenaseis close to zero indicating a complete andproper incorporation in the membrane and a preferentialregulation of the enzyme by a proton gradientrather than a membrane potential.Treatment of reconstituted transhydrogenase withN,N-dicyclohexylcarbodiimide results in an inhibitionof proton pump activity without an effect on uncoupledcatalytic activity, suggestingt hat proton translocationand catalytic activities are not obligatory linked orthat this agent separates proton pumping from thecatalytic activity. 

  • 41.
    Persson, Bengt L.
    et al.
    Department of Biochemistry, Arrhenius Laboratory, University of Stockholm.
    Hartog, A F
    Rydström, J
    Berden, J
    NBD-Cl modification of essential residues in mitochondrial nicotinamide nucleotide transhydrogenase from beef heart1988In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, ISSN 0167-4838, E-ISSN 1879-2588, Vol. 953, p. 241-248Article in journal (Refereed)
    Abstract [en]

    Modification of mitochondrial nicotinamide nucleotide transhydrogenase (NADPH:NAD+ oxidoreductase, EC 1.6.1.1) with 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl), followed by measurement of the absorption or fluorescence of the transhydrogenase-NBD adducts, resulted in a biphasic labelling of approx. 4–6 sulfhydryls, presumably cysteine residues. Of these 1–2 (27%) were fast-reacting and 3–4 (73%) slow-reacting sulfhydryls. In the presence of substrates, e.g., NADPH, the labelling was monophasic and all sulfhydryls were fast-reacting, suggesting that the modified sulfhydryls are predominantly localized peripheral to the NAD(P)(H)-binding sites. The rates of modification allowed the calculation of the rate constants for each phase of the labelling. Both in the absence and in the presence of a substrate, e.g., NADPH, the extent of labelling essentially parallelled the inhibition of transhydrogenase activity. Attempts to reactivate transhydrogenase by reduction of labelled sulfhydryls were not successful. Photo-induced transfer of the NBD adduct in partially inhibited transhydrogenase, from the sulfhydryls to reactive NH2 groups of amino-acid residue(s), identified as lysine residue(s), was parallelled by an inhibition of the residual transhydrogenase activity. It is suggested that a lysine localized close to the fast-reacting NBD-Cl-reactive sulfhydryl groups is essential for activity. 

  • 42.
    Persson, Bengt L.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Lagerstedt, J O
    Pratt, J R
    Pattison-Granberg, J
    Lundh, K
    Shokrollahzadeh, S
    Regulation of Phosphate Acquisition in Saccharomyces cerevisiae2003In: Current genetics, Vol. 43, p. 225-244Article in journal (Refereed)
  • 43.
    Persson, Bengt L.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Petersson, J
    Fristedt, U
    Weinander, R
    Berhe, A
    Pattison, J
    Phosphate Permeases of Saccharomyces cerevisiae: Structure, Function and Regulation1999In: Biochimica et biophysica acta, Vol. 1422, p. 255-272Article in journal (Refereed)
  • 44.
    Persson, Bengt L.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Roepe, P D
    Patel, L
    Lee, J
    Kaback, H R
    Site-directed mutagenesis of lysine 319 in the lactose permease of Escherichia coli1992In: Biochemistry, Vol. 31, p. 8892-8897Article in journal (Refereed)
  • 45.
    Persson, Bengt L.
    et al.
    UNIV STOCKHOLM, ARRHENIUS LAB, DEPT BIOCHEM.
    Rydström, J
    Evidence for a role of a vicinal dithiol in catalysis and proton pumping in mitochondrial nicotinamide nucleotide transhydrogenase1987In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 142, no 2, p. 573-578Article in journal (Refereed)
  • 46.
    Persson, Bengt L.
    et al.
    Department of Biochemistry and Biotechnology, Royal Institute of Technology .
    Rydström, J
    Kubista, M
    A circular dichroism study of mitochondrial transhydrogenase from beef heart1991In: Biophysical Chemistry, ISSN 0301-4622, E-ISSN 1873-4200, Vol. 39, no 3, p. 267-272Article in journal (Refereed)
    Abstract [en]

    This paper describes a circular dichroism (CD) spectroscopy study of purified proton-pumping nicotinamide nucleotide transhydrogenase from beef heart. The CD spectrum obtained was used to estimate the content of secondary structures of the purified enzyme and suggests the presence of 40–45% α-helical structure and long, possibly membrane-spanning α-helices. The spectrum was essentially unaffected by the absence or presence of transhydrogenase substrates, suggesting that the catalytic and proton-translocating activities of the enzyme occur without major rearrangements at the level of secondary structures. 

  • 47.
    Persson, Bengt L.
    et al.
    UNIV STOCKHOLM, DEPT BIOCHEM.
    Teixera da Cruz, A
    Rydström, J
    Energy-dependent interaction of substrates with mitochondrial nicotinamide nucleotide transhydrogenase1986In: Chemica Scripta, ISSN 0004-2056, Vol. 26, no 4, p. 581-584Article in journal (Refereed)
  • 48. Petersson, J
    et al.
    Pattison, J
    Kruckeberg, A L
    Berden, J
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Intracellular Localization of an Active Green Fluorescent Protein-Tagged Pho84 Phosphate Permease in Saccharomyces cerevisiae1999In: FEBS Letters, Vol. 462, p. 37-42Article in journal (Refereed)
  • 49. Petronilli, V
    et al.
    Persson, Bengt L.
    2Howard Hughes Medical Institute Research Laboratories, Molecular Biology Institute, University of California, Los Angeles, CA (U.S.A.).
    Zoratti, M
    Rydström, J
    Azzone, G F
    Flow-force relationships during energy transfer between mitochondrial proton pumps1991In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1058, no 2, p. 297-303Article in journal (Refereed)
    Abstract [en]

    The effect of inhibitors of proton pumps, of uncouplers and of permeant ions on the relationship between input force, , and output flows of the ATPase, redox and transhydrogenase H+-pumps in submitochondrial particles was investigated. It is concluded that: (1) The decrease of output flow of the transhydrogenase proton pump, defined as the rate of reduction of NADP+ by NADH, is linearily correlated with the decrease of input force, , in an extended range of , independently of whether the H+-generating pump is the ATPase or a redox pump, or whether is depressed by inhibitors of the H+-generating pump such as oligomycin or malonate, or by uncouplers. (2) The output flows of the ATPase and of the site I redox H+-pumps exhibit a steep dependence on . The flow-force relationships differ depending on whether the depression of is induced by inhibitors of the H+-generating pump, by uncouplers or by lipophilic anions. (3) With the ATPase as H+-consuming pump, at equivalent values, the output flow is more markedly inhibited by malonate than by uncouplers; the latter, however, are more inhibitory than lipophilic anions such as ClO4−. With redox site I as proton-consuming pump, at equivalent values, the output flow is more markedly inhibited by oligomycin than by uncouplers; again, uncouplers are more inhibitory than ClO4−. (4) The results provide further support for a delocalized interaction of transhydrogenase with other H+-pumps. 

  • 50. Pratt, J R
    et al.
    Mouillon, J M
    Lagerstedt, J O
    Pattison-Granberg, J
    Lundh, K
    Persson, Bengt L.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    The effect of methylphosphonate, a phosphate analog, on the expression and regulation of the high-affinity phosphate transporter Pho84 in Saccharomyces cerevisiae2004In: Biochemistry, Vol. 43, p. 14444-14453Article in journal (Refereed)
12 1 - 50 of 75
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