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© Research
Publication : Journal of Bacteriology

Localization of FtsI to the septal ring requires the Z ring, FtsA, FtsQ, and FtsL. Journal of Bacteriology 181:508-20.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of Bacteriology - 01 Jan 1999

Weiss D.S., Chen J.C., Ghigo J.-M., Boyd D., Beckwith J.

Link to Pubmed [PMID] – 9882665

J Bacteriol. 1999 Jan;181(2):508-20.

Assembly of the division septum in bacteria is mediated by several proteins that localize to the division site. One of these, FtsI (also called penicillin-binding protein 3) of Escherichia coli, consists of a short cytoplasmic domain, a single membrane-spanning segment, and a large periplasmic domain that encodes a transpeptidase activity involved in synthesis of septal peptidoglycan. We have constructed a merodiploid strain with a wild-type copy of ftsI at the normal chromosomal locus and a genetic fusion of ftsI to the green fluorescent protein (gfp) at the lambda attachment site. gfp-ftsI was expressed at physiologically appropriate levels under control of a regulatable promoter. Consistent with previous results based on immunofluorescence microscopy GFP-FtsI localized to the division site during the later stages of cell growth and throughout septation. Localization of GFP-FtsI to the cell pole(s) was not observed unless the protein was overproduced about 10-fold. Membrane anchor alterations shown previously to impair division but not membrane insertion or transpeptidase activity were found to interfere with localization of GFP-FtsI to the division site. In contrast, GFP-FtsI localized well in the presence of beta-lactam antibiotics that inhibit the transpeptidase activity of FtsI. Septal localization depended upon every other division protein tested (FtsZ, FtsA, FtsQ, and FtsL). We conclude that FtsI is a late recruit to the division site, and that its localization depends on an intact membrane anchor.

https://www.ncbi.nlm.nih.gov/pubmed/9882665