Analysis of the essential cell division gene ftsL of Bacillus subtilis by mutagenesis and heterologous complementation.

ABSTRACT: The ftsL gene is required for the initiation of cell division in a broad range of bacteria. Bacillus subtilis ftsL encodes a 13-kDa protein with a membrane-spanning domain near its N terminus. The external C-terminal domain has features of an alpha-helical leucine zipper, which is likely to be involved in the heterodimerization with another division protein, DivIC. To determine what residues are important for FtsL function, we used both random and site-directed mutagenesis. Unexpectedly, all chemically induced mutations fell into two clear classes, those either weakening the ribosome-binding site or producing a stop codon. It appears that the random mutagenesis was efficient, so many missense mutations must have been generated but with no phenotypic effect. Substitutions affecting hydropho

SUBMITTER: Sievers J 

PROVIDER: S-EPMC111003 | biostudies-literature | 2000 Oct

REPOSITORIES: biostudies-literature