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Periodicum biologorum, Vol.118 No.4 March 2017.

Short communication, Note
https://doi.org/10.18054/pb.v118i4.4572

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

Abderahmane Derouiche ; Systems and Synthetic Biology, Department of Biology and Biological Engineering, Chalmers University of Technology, Gothenburg
Dina Petranovic ; Systems and Synthetic Biology, Department of Biology and Biological Engineering, Chalmers University of Technology, Gothenburg
Boris Macek ; Proteome Center Tuebingen, Interfaculty Institute for Cell Biology, University of Tuebingen, Tuebingen
Ivan Mijakovic ; Systems and Synthetic Biology, Department of Biology and Biological Engineering, Chalmers University of Technology, Gothenburg, Sweden and Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Lyngby, Denmark

Fulltext: english, PDF (2 MB) pages 399-404 downloads: 154* cite
APA 6th Edition
Derouiche, A., Petranovic, D., Macek, B. & Mijakovic, I. (2016). Bacillus subtilis single-stranded DNA-binding protein SsbA is phosphorylated at threonine 38 by the serine/threonine kinase YabT. Periodicum biologorum, 118 (4), 399-404. https://doi.org/10.18054/pb.v118i4.4572
MLA 8th Edition
Derouiche, Abderahmane, et al. "Bacillus subtilis single-stranded DNA-binding protein SsbA is phosphorylated at threonine 38 by the serine/threonine kinase YabT." Periodicum biologorum, vol. 118, no. 4, 2016, pp. 399-404. https://doi.org/10.18054/pb.v118i4.4572. Accessed 10 Dec. 2018.
Chicago 17th Edition
Derouiche, Abderahmane, Dina Petranovic, Boris Macek and Ivan Mijakovic. "Bacillus subtilis single-stranded DNA-binding protein SsbA is phosphorylated at threonine 38 by the serine/threonine kinase YabT." Periodicum biologorum 118, no. 4 (2016): 399-404. https://doi.org/10.18054/pb.v118i4.4572
Harvard
Derouiche, A., et al. (2016). 'Bacillus subtilis single-stranded DNA-binding protein SsbA is phosphorylated at threonine 38 by the serine/threonine kinase YabT', Periodicum biologorum, 118(4), pp. 399-404. doi: https://doi.org/10.18054/pb.v118i4.4572
Vancouver
Derouiche A, Petranovic D, Macek B, Mijakovic I. Bacillus subtilis single-stranded DNA-binding protein SsbA is phosphorylated at threonine 38 by the serine/threonine kinase YabT. Periodicum biologorum [Internet]. 2016 [cited 2018 December 10];118(4):399-404. doi: https://doi.org/10.18054/pb.v118i4.4572
IEEE
A. Derouiche, D. Petranovic, B. Macek and I. Mijakovic, "Bacillus subtilis single-stranded DNA-binding protein SsbA is phosphorylated at threonine 38 by the serine/threonine kinase YabT", Periodicum biologorum, vol.118, no. 4, pp. 399-404, 2016. [Online]. doi: https://doi.org/10.18054/pb.v118i4.4572

Abstracts

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.

Hrčak ID: 177546

URI
https://hrcak.srce.hr/177546

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