期刊
INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY
卷 307, 期 1, 页码 1-10出版社
ELSEVIER GMBH, URBAN & FISCHER VERLAG
DOI: 10.1016/j.ijmm.2016.12.001
关键词
Staphylococcus aureus; Serine/threonine protein kinase; Lipid II; Cell division; Phosphorylation
资金
- German Research Foundation (DFG) [SCHN 1284/1-2]
- German Center for Infection Research (DZIF)
- Juergen Manchot Foundation
The assembly of the bacterial cell wall requires synchronization of a multitude of biosynthetic machineries and regulatory networks. The eukaryotic-like serine/threonine kinase PknB has been implicated in coordinating cross-wall formation, autolysis and cell division in Staphylococcus aureus. However, the signal molecule sensed by this kinase remained elusive so far. Here, we provide compelling biochemical evidence that PknB interacts with the ultimate cell wall precursor lipid II, triggering kinase activity. Moreover, we observed crosstalk of PknB with the two component system Wa1KR and identified the early cell division protein FtsZ as another PknB phosphorylation substrate in S. aureus. In agreement with the implied role in regulation of cell envelope metabolism, we found PknB to preferentially localize to the septum of S. aureus and the PASTA domains to be crucial for recruitment to this site. The data provide a model for the contribution of PknB to control cell wall metabolism and cell division. (C) 2016 Elsevier GmbH. All rights reserved.
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