The cell wall precursor lipid II acts as a molecular signal for the Ser/Thr kinase PknB of Staphylococcus aureus

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• 作者：Patrick Hardt^a ; Ina Engels^a ; ^b ; Marvin Rausch^a ; ^b ; Mike Gajdiss^c ; Hannah Ulm^a ; Peter Sass^d ; Knut Ohlsen^e ; Hans-Georg Sahl^b ; ^c ; Gabriele Bierbaum^c ; Tanja Schneider^a ; ^b ; ¹ ; ^{tanja@microbiology-bonn.de} ; Fabian Grein^a ; ^b ; ¹ ; ^{grein@uni-bonn.de}
• 关键词：TCS ; two-component regulatory system ; ESTK ; eukaryote-like serine/threonine kinase ; ESTP ; eukaryote-like serine/threonine phosphatase ; PASTA ; penicillin-binding protein and Ser/Thr kinase&ndash ; associated ; MRSA ; methicillin-resistant S. aureus ; PG ; peptidoglycan ; FR ; ratio of fluorescence ; SD ; standard deviation
• 刊名：International Journal of Medical Microbiology
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：307
• 期：1
• 页码：1-10
• 全文大小：1379 K
• 卷排序：307

文摘

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 WalKR 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.