WFRF:(Petranovic Nielsen Dina 1975)
Sökning: WFRF:(Petranovic Nielsen Dina 1975) > Bacillus subtilis s...
Bacillus subtilis single-stranded DNA-binding protein SsbA is phosphorylated at threonine 38 by the serine/threonine kinase YabT
-
- Derouiche, Abderahmane, 1980 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
-
- Petranovic Nielsen, Dina, 1975 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
-
- Macek, B. (författare)
- Eberhard Karls Universität Tübingen,Eberhard Karls University of Tübingen
- visa fler...
- visa färre...
- (creator_code:org_t)
- 2017-03-17
- 2016
- Engelska.
- Ingår i: Periodicum Biologorum. - : Hrvatski Prirodoslovno Drustvo (Croatian Society for Natural Sciences). - 0031-5362 .- 1849-0964. ; 118:4, s. 399-404
- Tidskriftsartikel (refereegranskat)
Abstract
Ämnesord
Stäng
- © 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
- NATURVETENSKAP -- Biologi -- Bioinformatik och systembiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Bioinformatics and Systems Biology (hsv//eng)
Nyckelord
- Mass spectrometry
- DNA metabolism cooperative binding
- Protein phosphorylation
- Protein kinase
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
Hitta mer i SwePub
- Av författaren/redakt...
- Derouiche, Abder ...
- Petranovic Niels ...
- Macek, B.
- Mijakovic, Ivan, ...
- Om ämnet
-
- NATURVETENSKAP
- NATURVETENSKAP
- och Biologi
- och Bioinformatik oc ...
- Artiklar i publikationen
- Periodicum Biolo ...
- Av lärosätet
- Chalmers tekniska högskola
Sök utanför SwePub
- Sök vidare i:
- Google Book Search
- Google Scholar
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.
- Copyright © LIBRIS - Nationella bibliotekssystem
- LIBRIS.kb.se
