例如:"lncRNA", "apoptosis", "WRKY"

Free SepF interferes with recruitment of late cell division proteins.

Sci Rep. 2017 Dec 05;7(1):16928
Yongqiang Gao 1 , Michaela Wenzel 1 , Martijs J Jonker 2 , Leendert W Hamoen 3
Yongqiang Gao 1 , Michaela Wenzel 1 , Martijs J Jonker 2 , Leendert W Hamoen 3

[No authors listed]

Author information
  • 1 Swammerdam Institute for Life Sciences, University of Amsterdam, O|2 Building, De Boelelaan 1108, 1081 HZ, Amsterdam, The Netherlands.
  • 2 MicroArray Department and Integrative Bioinformatics Unit, Swammerdam Institute for Life Sciences, University of Amsterdam, Sciencepark 904, 1098 XH, Amsterdam, The Netherlands.
  • 3 Swammerdam Institute for Life Sciences, University of Amsterdam, O|2 Building, De Boelelaan 1108, 1081 HZ, Amsterdam, The Netherlands. l.w.hamoen@uva.nl.

摘要


The conserved cell division protein SepF aligns polymers of FtsZ, the key cell division protein in bacteria, during synthesis of the (Fts)Z-ring at midcell, the first stage in cytokinesis. In addition, SepF acts as a membrane anchor for the Z-ring. Recently, it was shown that SepF overexpression in Mycobacterium smegmatis blocks cell division. Why this is the case is not known. Surprisingly, we found in Bacillus subtilis that SepF overproduction does not interfere with Z-ring assembly, but instead blocks assembly of late division proteins responsible for septum synthesis. Transposon mutagenesis suggested that SepF overproduction suppresses the essential WalRK two-component system, which stimulates expression of ftsZ. Indeed, it emerged that SepF overproduction impairs normal WalK localization. However, transcriptome analysis showed that the WalRK activity was in fact not reduced in SepF overexpressing cells. Further experiments indicated that SepF competes with EzrA and FtsA for binding to FtsZ, and that binding of extra SepF by FtsZ alleviates the cell division defect. This may explain why activation of WalRK in the transposon mutant, which increases ftsZ expression, counteracts the division defect. In conclusion, our data shows that an imbalance in early cell division proteins can interfere with recruitment of late cell division proteins.