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Bacillus subtilis single-stranded DNA-binding protein SsbA is phosphorylated at threonine 38 by the serine/threonine kinase YabT

Abderahmane Derouiche (Institutionen för biologi och bioteknik, Systembiologi) ; Dina Petranovic (Institutionen för biologi och bioteknik, Systembiologi) ; B. Macek ; Ivan Mijakovic (Institutionen för biologi och bioteknik, Systembiologi)
Periodicum Biologorum (0031-5362). Vol. 118 (2016), 4, p. 399-404.
[Artikel, refereegranskad vetenskaplig]

© 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.

Nyckelord: DNA metabolism cooperative binding, Mass spectrometry, Protein kinase, Protein phosphorylation



Denna post skapades 2017-04-27. Senast ändrad 2017-05-09.
CPL Pubid: 248988

 

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Institutioner (Chalmers)

Institutionen för biologi och bioteknik, Systembiologi

Ämnesområden

Bioinformatik och systembiologi

Chalmers infrastruktur