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Bacillus subtilis s...
Bacillus subtilis single-stranded DNA-binding protein SsbA is phosphorylated at threonine 38 by the serine/threonine kinase YabT
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- Derouiche, Abderahmane, 1980 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Petranovic Nielsen, Dina, 1975 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Macek, B. (author)
- Eberhard Karls Universität Tübingen,Eberhard Karls University of Tübingen
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- Mijakovic, Ivan, 1975 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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(creator_code:org_t)
- 2017-03-17
- 2016
- English.
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In: Periodicum Biologorum. - : Hrvatski Prirodoslovno Drustvo (Croatian Society for Natural Sciences). - 0031-5362 .- 1849-0964. ; 118:4, s. 399-404
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Abstract
Subject headings
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- © 2016, Croatian Society of Natural Sciences. All rights reserved.Background and purpose: Single-stranded DNA-binding proteins participate in all stages of DNA metabolism that involve single-stranded DNA, from replication, recombination, repair of DNA damage, to natural competence in species such as Bacillus subtilis. B. subtilis single-stranded DNA-binding proteins have previously been found to be phosphorylated on tyrosine and arginine residues. While tyrosine phosphorylation was shown to enhance the DNA-binding properties of SsbA, arginine phosphorylation was not functionally characterized. Materials and methods: We used mass spectrometry analysis to detect phosphorylation of SsbA purified from B. subtilis cells. The detected phosphorylation site was assessed for its influence on DNA-binding in vitro, using electrophoretic mobility shift assays. The ability of B. subtilis serine/ threonine kinases to phosphorylate SsbA was assessed using in vitro phosphorylation assays. Results: In addition to the known tyrosine phosphorylation of SsbA on tyrosine 82, we identified a new phosphorylation site: threonine 38. The in vitro assays demonstrated that SsbA is preferentially phosphorylated by the B. subtilis Hanks-type kinase YabT, and phosphorylation of threonine 38 leads to enhanced cooperative binding to DNA. Conclusions: Our findings contribute to the emerging picture that bacterial proteins, exemplified here by SsbA, undergo phosphorylation at multiple residues. This results in a complex regulation of cellular functions, and suggests that the complexity of the bacterial cellular regulation may be underestimated.
Subject headings
- NATURVETENSKAP -- Biologi -- Bioinformatik och systembiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Bioinformatics and Systems Biology (hsv//eng)
Keyword
- Protein phosphorylation
- Protein kinase
- Mass spectrometry
- DNA metabolism cooperative binding
Publication and Content Type
- art (subject category)
- ref (subject category)
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