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Regulated intramembrane proteolysis of FtsL protein and the control of cell division in Bacillus subtilis
Author(s) -
Bramkamp Marc,
Weston Louise,
Daniel Richard A.,
Errington Jeff
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.1365-2958.2006.05402.x
Subject(s) - biology , bacillus subtilis , cell division , metalloproteinase , proteolysis , proteases , microbiology and biotechnology , protease , serine protease , genetics , biochemistry , cell , enzyme , bacteria
Summary The small bitopic division protein FtsL is an essential part of the division machinery (divisome) in most eubacteria. In Bacillus subtilis FtsL is a highly unstable protein and the turnover has been implicated in regulation of division in response to DNA damage. N‐terminal deletions and a domain swap experiment identified the short cytoplasmic domain of FtsL as being required for instability. We then identified a zinc metalloprotease, YluC, required for turnover, and likely sequence motifs involved in substrate recognition. YluC belongs to the site‐2‐protease (S2P) family of proteases involved in regulated intramembrane proteolysis (RIP), which plays a role in diverse regulatory phenomena from bacteria to man. The yluC mutant, and strains with N‐terminal truncations of ftsL have a short cell phenotype, indicating that that FtsL is normally rate‐limiting for division. Coexpression experiments of FtsL and YluC in Escherichia coli corroborated a model in which FtsL is directly cleaved by the membrane metalloprotease. The results shed new light on the regulation of cell division in B. subtilis and identify a novel class of targets for RIP.