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A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis.
- Source :
-
Molecular Microbiology . Jun2006, Vol. 60 Issue 6, p1364-1380. 17p. 6 Diagrams, 1 Chart. - Publication Year :
- 2006
-
Abstract
- The assembly of ring-like structures, composed of FtsZ proteins (i.e. the Z ring), is the earliest and most essential process in bacterial cytokinesis. It has been shown that this process is directly regulated by the FtsZ-binding proteins, FtsA, ZapA, and EzrA, in Bacillus subtilis. In this study, protein complexes that are involved in Z-ring formation were chemically cross-linked in vivo, purified by affinity chromatography, and analysed by mass spectrometry. Analysis of the results identified YlmF as a new component of the FtsZ complex. Yeast two-hybrid analysis and fluorescence microscopy of YFP–YlmF in B. subtilis cells indicated YlmF localizes to the division site in an FtsZ-dependent manner. A single disruption of YlmF resulted in a slight elongation of cells; however, simultaneous inactivation of both YlmF and FtsA showed synthetic lethality caused by complete blockage of cell division due to the defect in Z-ring formation. In contrast, the ftsA-null mutant phenotype, caused by inefficient Z-ring formation, could be complemented by overexpression of YlmF. These results suggest that YlmF has an overlapping function with FtsA in stimulating the formation of Z rings in B. subtilis. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 0950382X
- Volume :
- 60
- Issue :
- 6
- Database :
- Academic Search Index
- Journal :
- Molecular Microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 20923964
- Full Text :
- https://doi.org/10.1111/j.1365-2958.2006.05184.x