Affiliation:
1. Department of Microbiology, University of Iowa, Iowa City, Iowa 52242
2. Department of Veterinary Microbiology, Veterinary Medical Research Institute, Iowa State University, Ames, Iowa 50011-1240
Abstract
ABSTRACT
FtsE and FtsX have homology to the ABC transporter superfamily of proteins and appear to be widely conserved among bacteria. Early work implicated FtsEX in cell division in
Escherichia coli
, but this was subsequently challenged, in part because the division defects in
ftsEX
mutants are often salt remedial. Strain RG60 has an
ftsE
::
kan
null mutation that is polar onto
ftsX
. RG60 is mildly filamentous when grown in standard Luria-Bertani medium (LB), which contains 1% NaCl, but upon shift to LB with no NaCl growth and division stop. We found that FtsN localizes to potential division sites, albeit poorly, in RG60 grown in LB with 1% NaCl. We also found that in wild-type
E. coli
both FtsE and FtsX localize to the division site. Localization of FtsX was studied in detail and appeared to require FtsZ, FtsA, and ZipA, but not the downstream division proteins FtsK, FtsQ, FtsL, and FtsI. Consistent with this, in media lacking salt, FtsA and ZipA localized independently of FtsEX, but the downstream proteins did not. Finally, in the absence of salt, cells depleted of FtsEX stopped dividing before any change in growth rate (mass increase) was apparent. We conclude that FtsEX participates directly in the process of cell division and is important for assembly or stability of the septal ring, especially in salt-free media.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
175 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献