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A new FtsZ‐interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis
Author(s) -
Ishikawa Shu,
Kawai Yoshikazu,
Hiramatsu Konosuke,
Kuwano Masayoshi,
Ogasawara Naotake
Publication year - 2006
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2006.05184.x
Subject(s) - ftsz , bacillus subtilis , cytokinesis , biology , cell division , mutant , microbiology and biotechnology , biochemistry , cell , genetics , bacteria , gene
Summary 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 .