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- Derouiche, Abderahmane,1980Chalmers tekniska högskola,Chalmers University of Technology (författare)
Bacillus subtilis single-stranded DNA-binding protein SsbA is phosphorylated at threonine 38 by the serine/threonine kinase YabT
- Artikel/kapitelEngelska2016
Förlag, utgivningsår, omfång ...
- 2017-03-17
- Hrvatski Prirodoslovno Drustvo (Croatian Society for Natural Sciences),2016
Nummerbeteckningar
- LIBRIS-ID:oai:research.chalmers.se:e45a75e5-2cf3-438f-aea2-b593ca3ecfeb
- https://doi.org/10.18054/pb.v118i4.4572DOI
- https://research.chalmers.se/publication/248988URI
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- Språk:engelska
- Sammanfattning på:engelska
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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.
Ämnesord och genrebeteckningar
- NATURVETENSKAP Biologi Bioinformatik och systembiologi hsv//swe
- NATURAL SCIENCES Biological Sciences Bioinformatics and Systems Biology hsv//eng
- Mass spectrometry
- DNA metabolism cooperative binding
- Protein phosphorylation
- Protein kinase
Biuppslag (personer, institutioner, konferenser, titlar ...)
- Petranovic Nielsen, Dina,1975Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)dinap (författare)
- Macek, B.Eberhard Karls Universität Tübingen,Eberhard Karls University of Tübingen (författare)
- Mijakovic, Ivan,1975Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)ivanmi (författare)
- Chalmers tekniska högskolaEberhard Karls Universität Tübingen (creator_code:org_t)
Sammanhörande titlar
- Ingår i:Periodicum Biologorum: Hrvatski Prirodoslovno Drustvo (Croatian Society for Natural Sciences)118:4, s. 399-4040031-53621849-0964
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