title: DivIC stabilizes FtsL against RasP cleavage.
abstract: The essential cell division protein FtsL is a substrate of the intramembrane protease RasP. Using heterologous coexpression experiments, we show here that the division protein DivIC stabilizes FtsL against RasP cleavage. Degradation seems to be initiated upon accessibility of a cytosolic substrate recognition motif.
authors.affiliation: Institute for Biochemistry, University of Cologne, Zülpicher Str. 47, Cologne D-50674, Germany.
authors.forename: Inga
authors.initials: I
authors.lastname: Wadenpohl
authors.forename: Marc
authors.initials: M
authors.lastname: Bramkamp
mesh_terms: D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D001426:Bacterial Proteins