Papers

Peer-reviewed Lead author
Feb, 2008

Compensation for the loss of the conserved membrane targeting sequence of FtsA provides new insights into its function

MOLECULAR MICROBIOLOGY
  • Daisuke Shiomi
  • ,
  • William Margolin

Volume
67
Number
3
First page
558
Last page
569
Language
English
Publishing type
Research paper (scientific journal)
DOI
10.1111/j.1365-2958.2007.06085.x
Publisher
BLACKWELL PUBLISHING

The bacterial actin homologue FtsA has a conserved C-terminal membrane targeting sequence (MTS). Deletion or point mutations in the MTS, such as W408E, were shown previously to inactivate FtsA function and inhibit cell division. Because FtsA binds to the tubulin-like FtsZ protein that forms the Z ring, it is thought that the MTS of FtsA is required, along with the transmembrane protein ZipA, to assemble the Z ring and anchor it to the cytoplasmic membrane. Here, we show that despite its reduced membrane binding, FtsA-W408E could localize to the Z ring and recruit the late cell division protein FtsI, but was defective in self-interaction and recruitment of FtsN, another late cell division protein. These defects could be suppressed by a mutation that stimulates membrane association of FtsA-W408E, or by expressing a tandem FtsA-W408E. Remarkably, the FtsA MTS could be completely replaced with the transmembrane domain of MalF and remain functional for cell division. We propose that FtsA function in cell division depends on additive effects of membrane binding and self-interaction, and that the specific requirement of an amphipathic helix for tethering FtsA to the membrane can be bypassed.

Link information
DOI
https://doi.org/10.1111/j.1365-2958.2007.06085.x
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/18186792
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000252175600008&DestApp=WOS_CPL
ID information
  • DOI : 10.1111/j.1365-2958.2007.06085.x
  • ISSN : 0950-382X
  • Pubmed ID : 18186792
  • Web of Science ID : WOS:000252175600008

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