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Persson, Bengt L.
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Samyn, D. R. & Persson, B. L. (2016). Inorganic phosphate and sulfate transport in S. cerevisiae. In: José Ramos, Hana Sychrova, Maik Kschischo (Ed.), Yeast Membrane Transport: (pp. 253-269). Springer
Öppna denna publikation i ny flik eller fönster >>Inorganic phosphate and sulfate transport in S. cerevisiae
2016 (Engelska)Ingår i: Yeast Membrane Transport / [ed] José Ramos, Hana Sychrova, Maik Kschischo, Springer, 2016, s. 253-269Kapitel i bok, del av antologi (Refereegranskat)
Abstract [en]

Inorganic ions such as phosphate and sulfate are essential macronutrients required for a broad spectrum of cellular functions and their regulation. In a constantly fluctuating environment microorganisms have for their survival developed specific nutrient sensing and transport systems ensuring that the cellular nutrient needs are met. This chapter focuses on the S. cerevisiae plasma membrane localized transporters, of which some are strongly induced under conditions of nutrient scarcity and facilitate the active uptake of inorganic phosphate and sulfate. Recent advances in studying the properties of the high-affinity phosphate and sulfate transporters by means of site-directed mutagenesis have provided further insight into the molecular mechanisms contributing to substrate selectivity and transporter functionality of this important class of membrane transporters.

Ort, förlag, år, upplaga, sidor
Springer, 2016
Serie
Advances in Experimental Medicine and Biology, ISSN 0065-2598 ; 892
Nyckelord
Phosphate, Regulation, S. cerevisiae, Sulfate, Transport
Nationell ämneskategori
Biokemi och molekylärbiologi
Forskningsämne
Kemi, Biokemi
Identifikatorer
urn:nbn:se:lnu:diva-47551 (URN)10.1007/978-3-319-25304-6_10 (DOI)000370774200010 ()26721277 (PubMedID)2-s2.0-84953262969 (Scopus ID)9783319253022 (ISBN)9783319253046 (ISBN)
Tillgänglig från: 2015-11-25 Skapad: 2015-11-25 Senast uppdaterad: 2019-08-09Bibliografiskt granskad
Samyn, D. R., Van der Veken, J., Van Zeebroeck, G., Persson, B. L. & Karlsson, B. C. G. (2016). Key Residues and Phosphate Release Routes in the Saccharomyces cerevisae Pho84 Transceptor - The Role of Tyr179 in Functional Regulation. Journal of Biological Chemistry, 291(51), 26388-26398
Öppna denna publikation i ny flik eller fönster >>Key Residues and Phosphate Release Routes in the Saccharomyces cerevisae Pho84 Transceptor - The Role of Tyr179 in Functional Regulation
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2016 (Engelska)Ingår i: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 291, nr 51, s. 26388-26398Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Pho84, a major facilitator superfamily (MFS) protein, is the main high-affinity Pi transceptor in Saccharomyces cerevisiae. Although transport mechanisms have been suggested for other MFS members, the key residues and molecular events driving transport by Pi: H+ symporters are unclear. The current Pho84 transport model is based on the inward-facing occluded crystal structure of the Pho84 homologue PiPT in the fungus Piriformospora indica. However, this model is limited by the lack of experimental data on the regulatory residues for each stage of the transport cycle. In this study, an open, inward-facing conformation of Pho84 was used to study the release of Pi. A comparison of this conformation with the model for Pi release in PiPT revealed that Tyr(179) in Pho84 (Tyr150 in PiPT) is not part of the Pi binding site. This difference may be due to a lack of detailed information on the Pi release step in PiPT. Molecular dynamics simulations of Pho84 in which a residue adjacent to Tyr(179), Asp(178), is protonated revealed a conformational change in Pho84 from an open, inward-facing state to an occluded state. Tyr(179) then became part of the binding site as was observed in the PiPT crystal structure. The importance of Tyr(179) in regulating Pi release was supported by site-directed mutagenesis and transport assays. Using trehalase activity measurements, we demonstrated that the release of Pi is a critical step for transceptor signaling. Our results add to previous studies on PiPT, creating a more complete picture of the proton-coupled Pi transport cycle of a transceptor.

Nyckelord
Pho84, Saccharomyces cerevisiae, Molecular dynamics, membrane protein, transport
Nationell ämneskategori
Biokemi och molekylärbiologi Biofysik
Forskningsämne
Kemi, Biokemi
Identifikatorer
urn:nbn:se:lnu:diva-60171 (URN)10.1074/jbc.M116.738112 (DOI)000391568200013 ()2-s2.0-85006241160 (Scopus ID)
Forskningsfinansiär
Crafoordska stiftelsen, 20150874Swedish National Infrastructure for Computing (SNIC), SNIC 2014/1-404 SNIC 2015/1-444
Tillgänglig från: 2017-01-24 Skapad: 2017-01-24 Senast uppdaterad: 2018-11-02Bibliografiskt granskad
Johri, A. K., Oelmueller, R., Dua, M., Yadav, V., Kumar, M., Tuteja, N., . . . Stroud, R. M. (2015). Fungal association and utilization of phosphate by plants: success, limitations, and future prospects. Frontiers in Microbiology, 6, Article ID 984.
Öppna denna publikation i ny flik eller fönster >>Fungal association and utilization of phosphate by plants: success, limitations, and future prospects
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2015 (Engelska)Ingår i: Frontiers in Microbiology, ISSN 1664-302X, E-ISSN 1664-302X, Vol. 6, artikel-id 984Artikel, forskningsöversikt (Refereegranskat) Published
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.

Nyckelord
phosphates, transporters, rhizosphere, phosphate transport proteins, phsophate uptake
Nationell ämneskategori
Mikrobiologi Botanik
Forskningsämne
Kemi, Biokemi
Identifikatorer
urn:nbn:se:lnu:diva-47381 (URN)10.3389/fmicb.2015.00984 (DOI)000363858500001 ()2-s2.0-84946818959 (Scopus ID)
Tillgänglig från: 2015-11-24 Skapad: 2015-11-24 Senast uppdaterad: 2018-11-16Bibliografiskt granskad
Sengottaiyan, P., Petrlova, J., Lagerstedt, J., Ruiz-Pavon, L., Budamagunta, M., Voss, J. & Persson, B. L. (2013). Characterization of the biochemical and biophysical properties of the Saccharomyces cerevisiae phosphate transporter Pho89. Biochemical and Biophysical Research Communications - BBRC, 436(3), 551-556
Öppna denna publikation i ny flik eller fönster >>Characterization of the biochemical and biophysical properties of the Saccharomyces cerevisiae phosphate transporter Pho89
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2013 (Engelska)Ingår i: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 436, nr 3, s. 551-556Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

In Saccharomyces cerevisiae, Pho89 mediates a cation-dependent transport of Pi across the plasma membrane. This integral membrane protein belongs to the Inorganic Phosphate Transporter (PiT) family, a group that includes the mammalian Na+/Pi cotransporters Pit1 and Pit2. Here we report that the Pichia pastoris expressed recombinant Pho89 was purified in the presence of Foscholine-12 and functionally reconstituted into proteoliposomes with a similar substrate specificity as observed in an intact cell system. The alpha-helical content of the Pho89 protein was estimated to 44%. EPR analysis showed that purified Pho89 protein undergoes conformational change upon addition of substrate. 

Ort, förlag, år, upplaga, sidor
Elsevier, 2013
Nyckelord
Pho89, Pichia pastoris, Oligomer, Reconstitution, Phosphate transport, Circular dichroism
Nationell ämneskategori
Kemi Biokemi och molekylärbiologi
Forskningsämne
Kemi, Biokemi
Identifikatorer
urn:nbn:se:lnu:diva-27720 (URN)10.1016/j.bbrc.2013.06.011 (DOI)000321995900034 ()2-s2.0-84879889835 (Scopus ID)
Projekt
Characterization of sensors and signal transduction in regulation of phosphate uptake systems
Forskningsfinansiär
Vetenskapsrådet, 621-2007-6144Vetenskapsrådet, 522-2008-3724,7480
Tillgänglig från: 2013-08-01 Skapad: 2013-08-01 Senast uppdaterad: 2018-11-16Bibliografiskt granskad
Sengottaiyan, P., Ruiz-Pavon, L. & Persson, B. L. (2013). Functional expression, purification and reconstitution of the recombinant phosphate transporter Pho89 of Saccharomyces cerevisiae. The FEBS Journal, 280(3), 965-975
Öppna denna publikation i ny flik eller fönster >>Functional expression, purification and reconstitution of the recombinant phosphate transporter Pho89 of Saccharomyces cerevisiae
2013 (Engelska)Ingår i: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 280, nr 3, s. 965-975Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The Saccharomyces cerevisiae high-affinity phosphate transporter Pho89 is a member of the inorganic phosphate (Pi) transporter (PiT) family, and shares significant homology with the type III Na+/Pi symporters, hPit1 and hPit2. Currently, detailed biochemical and biophysical analyses of Pho89 to better understand its transport mechanisms are limited, owing to the lack of purified Pho89 in an active form. In the present study, we expressed functional Pho89 in the cell membrane of Pichia pastoris, solubilized it in Triton X-100 and foscholine-12, and purified it by immobilized nickel affinity chromatography combined with size exclusion chromatography. The protein eluted as an oligomer on the gel filtration column, and SDS/PAGE followed by western blotting analysis revealed that the protein appeared as bands of approximately 63, 140 and 520 kDa, corresponding to the monomeric, dimeric and oligomeric masses of the protein, respec- tively. Proteoliposomes containing purified and reconstituted Pho89 showed Na+-dependent Pi transport activity driven by an artificially imposed electrochemical Na+ gradient. This implies that Pho89 operates as a symporter. Moreover, its activity is sensitive to the Na+ ionophore monensin. To our knowledge, this study represents the first report on the functional reconstitution of a Pi-coupled PiT family member. 

Ort, förlag, år, upplaga, sidor
Wiley-Blackwell, 2013
Nyckelord
Pho89, phosphate transport reconstitution, Pichia pastoris, Saccharomyces cerevisiae
Nationell ämneskategori
Biokemi och molekylärbiologi
Forskningsämne
Kemi, Biokemi
Identifikatorer
urn:nbn:se:lnu:diva-23435 (URN)10.1111/febs.12090 (DOI)000314167100015 ()23216645 (PubMedID)2-s2.0-84873160670 (Scopus ID)
Projekt
Karakterisering av sensorer och signalöverföring i reglering av cellulära fosfatupptagssystem
Forskningsfinansiär
Vetenskapsrådet, 621-2007-6144
Tillgänglig från: 2013-01-22 Skapad: 2013-01-14 Senast uppdaterad: 2017-12-06Bibliografiskt granskad
Samyn, D. R., Andersson, M., Ruiz-Pavon, L., Popova, Y., Persson, B. L. & Thevelein, J. (2013). The high-affinity inorganic phosphate transport system of Saccharomyces cerevisiae: a tale of two proteins. Paper presented at 38th Congress of the Federation-of-European-Biochemical-Societies (FEBS), JUL 06-11, 2013, Saint Petersburg, RUSSIA. The FEBS Journal, 280, 152-152
Öppna denna publikation i ny flik eller fönster >>The high-affinity inorganic phosphate transport system of Saccharomyces cerevisiae: a tale of two proteins
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2013 (Engelska)Ingår i: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 280, s. 152-152Artikel i tidskrift, Meeting abstract (Övrigt vetenskapligt) Published
Nationell ämneskategori
Biokemi och molekylärbiologi
Forskningsämne
Naturvetenskap, Biokemi
Identifikatorer
urn:nbn:se:lnu:diva-31011 (URN)000325919200473 ()
Konferens
38th Congress of the Federation-of-European-Biochemical-Societies (FEBS), JUL 06-11, 2013, Saint Petersburg, RUSSIA
Tillgänglig från: 2013-12-09 Skapad: 2013-12-06 Senast uppdaterad: 2017-12-06Bibliografiskt granskad
Schothorst, J., Nag Kankipati, H., Conrad, M., Samyn, D. R., Van Zeebroeck, G., Popova, Y., . . . Thevelein, J. (2013). Yeast nutrient transceptors provide novel insight in the functionality of membrane transporters.. Current Genetics, 59(4), 197-206
Öppna denna publikation i ny flik eller fönster >>Yeast nutrient transceptors provide novel insight in the functionality of membrane transporters.
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2013 (Engelska)Ingår i: Current Genetics, ISSN 0172-8083, E-ISSN 1432-0983, Vol. 59, nr 4, s. 197-206Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

In the yeast Saccharomyces cerevisiae several nutrient transporters have been identified that possess an additional function as nutrient receptor. These transporters are induced when yeast cells are starved for their substrate, which triggers entry into stationary phase and acquirement of a low protein kinase A (PKA) phenotype. Re-addition of the lacking nutrient triggers exit from stationary phase and sudden activation of the PKA pathway, the latter being mediated by the nutrient transceptors. At the same time, the transceptors are ubiquitinated, endocytosed and sorted to the vacuole for breakdown. Investigation of the signaling function of the transceptors has provided a new read-out and new tools for gaining insight into the functionality of transporters. Identification of amino acid residues that bind co-transported ions in symporters has been challenging because the inactivation of transport by site-directed mutagenesis is not conclusive with respect to the cause of the inactivation. The discovery of nontransported agonists of the signaling function in transceptors has shown that transport is not required for signaling. Inactivation of transport with maintenance of signaling in transceptors supports that a true proton-binding residue was mutagenised. Determining the relationship between transport and induction of endocytosis has also been challenging, since inactivation of transport by mutagenesis easily causes loss of all affinity for the substrate. The use of analogues with different combinations of transport and signaling capacities has revealed that transport, ubiquitination and endocytosis can be uncoupled in several unexpected ways. The results obtained are consistent with transporters undergoing multiple substrate-induced conformational changes, which allow interaction with different accessory proteins to trigger specific downstream events.

Ort, förlag, år, upplaga, sidor
Springer, 2013
Nationell ämneskategori
Biokemi och molekylärbiologi
Forskningsämne
Kemi, Biokemi
Identifikatorer
urn:nbn:se:lnu:diva-30016 (URN)10.1007/s00294-013-0413-y (DOI)000325942600004 ()2-s2.0-84886856582 (Scopus ID)
Forskningsfinansiär
Vetenskapsrådet, 621-2007-6144
Tillgänglig från: 2013-10-29 Skapad: 2013-10-29 Senast uppdaterad: 2018-11-16Bibliografiskt granskad
Momeni, N., Bergquist, J., Brudin, L., Behnia, F., Sivberg, B., Joghataei, M. & Persson, B. L. (2012). A novel blood-based biomarker for detection of autism spectrum disorders. Translational Psychiatry, 2, Article ID e91.
Öppna denna publikation i ny flik eller fönster >>A novel blood-based biomarker for detection of autism spectrum disorders
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2012 (Engelska)Ingår i: Translational Psychiatry, ISSN 2158-3188, E-ISSN 2158-3188, Vol. 2, artikel-id e91Artikel i tidskrift (Refereegranskat) Published
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. 

Ort, förlag, år, upplaga, sidor
Nature Publishing Group, 2012
Nyckelord
ASD, autism spectrum disorders, biomarker, blood
Nationell ämneskategori
Neurologi Biokemi och molekylärbiologi
Forskningsämne
Naturvetenskap, Biomedicinsk vetenskap
Identifikatorer
urn:nbn:se:lnu:diva-18964 (URN)10.1038/tp.2012.19 (DOI)2-s2.0-84858021906 (Scopus ID)
Tillgänglig från: 2012-05-28 Skapad: 2012-05-28 Senast uppdaterad: 2017-12-07Bibliografiskt granskad
Momeni, N., Brudin, L., Behnia, F., Nordström, B., Yousefi-Oudarji, A., Sivberg, B., . . . Persson, B. L. (2012). High complement factor I activity in the plasma of children with autism spectrum disorders. Autism Research and Treatment, Article ID 868576.
Öppna denna publikation i ny flik eller fönster >>High complement factor I activity in the plasma of children with autism spectrum disorders
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2012 (Engelska)Ingår i: Autism Research and Treatment, ISSN 2090-1925, E-ISSN 2090-1933, artikel-id 868576Artikel i tidskrift (Refereegranskat) Published
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.

Ort, förlag, år, upplaga, sidor
Hindawi Publishing Corporation, 2012
Nyckelord
Factor I, Autism Spectrum Disorders, ASD
Nationell ämneskategori
Immunologi inom det medicinska området Neurologi
Forskningsämne
Naturvetenskap, Biomedicinsk vetenskap
Identifikatorer
urn:nbn:se:lnu:diva-16722 (URN)10.1155/2012/868576 (DOI)
Projekt
Autism spectrum disorders
Tillgänglig från: 2012-01-11 Skapad: 2012-01-11 Senast uppdaterad: 2018-01-12Bibliografiskt granskad
Andersson, M. R., Samyn, D. R. & Persson, B. L. (2012). Mutational analysis of conserved glutamic acids of Pho89, a Saccharomyces cerevisiae high-affinity inorganic phosphate:Na+ symporter. Biologia (Bratislava), 67(6), 1056-1061
Öppna denna publikation i ny flik eller fönster >>Mutational analysis of conserved glutamic acids of Pho89, a Saccharomyces cerevisiae high-affinity inorganic phosphate:Na+ symporter
2012 (Engelska)Ingår i: Biologia (Bratislava), ISSN 0006-3088, E-ISSN 1336-9563, Vol. 67, nr 6, s. 1056-1061Artikel i tidskrift (Refereegranskat) Published
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.

Nyckelord
SLC20, Pho89, Saccharomyces cerevisiae, site-directed mutagenesis, inorganic phosphate transport
Nationell ämneskategori
Biokemi och molekylärbiologi
Forskningsämne
Naturvetenskap, Biokemi
Identifikatorer
urn:nbn:se:lnu:diva-22689 (URN)10.2478/s11756-012-0118-6 (DOI)000310087300004 ()2-s2.0-84867809909 (Scopus ID)
Tillgänglig från: 2012-12-05 Skapad: 2012-12-05 Senast uppdaterad: 2017-12-07Bibliografiskt granskad
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