Affiliation:
1. Department of Microbiology and Molecular Genetics, McGovern Medical School, Houston, Texas, USA
Abstract
Escherichia coli
cells divide using a cytokinetic ring composed of polymers of the tubulin-like FtsZ. To function properly, these polymers must attach to the inner surface of the cytoplasmic membrane via two essential membrane-associated tethers, FtsA and ZipA. Both FtsA and ZipA contain peptide linkers that connect their membrane-binding domains with their FtsZ-binding domains. Although they are presumed to be crucial for cell division activity, the importance of these linkers has not yet been rigorously tested. Here, we show that large segments of these linkers can be removed with few consequences for cell division, although several subtle defects were uncovered. Our results suggest that ZipA, in particular, can function in cell division without an extended linker.
Funder
John and Rebekah Harper Fellowship
Graduate School of Biomedical Sciences, University of Texas Health Science Center at Houston
HHS | NIH | Office of Extramural Research, National Institutes of Health
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
4 articles.
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