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Mutational analysis of putative phosphate- and proton-binding sites in the Saccharomyces cerevisiae Pho84 phosphate:H+ transceptor and its effect on signalling to the PKA and PHO pathways
Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences. (Bengt Persson)ORCID iD: 0000-0002-0381-251X
Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences. (Bengt Persson)
Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences. (Bengt Persson)
Katholieke Universiteit Leuven.
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2012 (English)In: Biochemical Journal, ISSN 0264-6021, E-ISSN 1470-8728, Vol. 445, 413-422 p.Article in journal (Refereed) Published
Abstract [en]

In Saccharomyces cerevisiae, the Pho84 phosphate transporter acts as the main provider of phosphate to the cell using a proton symport mechanism, but also mediates rapid activation of the PKA (protein kinase A) pathway. These two features led to recognition of Pho84 as a transceptor. Although the physiological role of Pho84 has been studied in depth, the mechanisms underlying the transport and sensor functions are unclear. To obtain more insight into the structure–function relationships of Pho84, we have rationally designed and analysed site-directed mutants. Using a three-dimensional model of Pho84 created on the basis of the GlpT permease, complemented with multiple sequence alignments, we selected Arg168 and Lys492, and Asp178, Asp358 and Glu473 as residues potentially involved in phosphate or proton binding respectively, during transport. We found that Asp358 (helix 7) and Lys492 (helix 11) are critical for the transport function, and might be part of the putative substrate-binding pocket of Pho84. Moreover, we show that alleles mutated in the putative proton-binding site Asp358 are still capable of strongly activating PKA pathway targets, despite their severely reduced transport activity. This indicates that signalling does not require transport and suggests that mutagenesis of amino acid residues involved in binding of the co-transported ion may constitute a promising general approach to separate the transport and signalling functions in transceptors.

Place, publisher, year, edition, pages
Portland Press , 2012. Vol. 445, 413-422 p.
Keyword [en]
Pho84, phosphate binding, phosphate transport, protein kinase A, proton binding, Saccharomyces cerevisiae, transceptor.
National Category
Biochemistry and Molecular Biology
Research subject
Natural Science, Biochemistry
Identifiers
URN: urn:nbn:se:lnu:diva-20897DOI: 10.1042/BJ20112086Scopus ID: 2-s2.0-84864360049OAI: oai:DiVA.org:lnu-20897DiVA: diva2:542018
Projects
Characterization of sensors and signal transduction in regulation of phosphate uptake systems
Funder
Swedish Research Council, 621-2007-6144
Available from: 2012-07-27 Created: 2012-07-27 Last updated: 2017-12-07Bibliographically approved

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Samyn, Dieter R.Ruiz-Pavon, LorenaAndersson, Michael R.Persson, Bengt L.

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