Abstract
Three genes from the Bacillus subtilis major che-fla operon have been cloned and sequenced. Two of the genes encode proteins that are homologous to the Escherichia coli and Salmonella typhimurium flagellar biosynthetic proteins FliP and FliQ. The third gene, designated fliZ, encodes a 219-amino-acid protein with a predicted molecular mass of 24,872 Da. FliZ is not significantly homologous to any known proteins. Null mutants in fliP and fliZ do not have flagella; however, motility can be restored to the fliZ null mutant by expression of fliZ from a plasmid. FliZ has a conventional N-terminal signal sequence that does not direct secretion of the protein but appears to target the protein to the membrane. Two possible models of insertion of FliZ into the membrane are described.
MeSH Terms
Amino Acid Sequence
Bacillus subtilis/genetics
Bacterial Proteins/chemistry,genetics
Base Sequence
Blotting, Southern
Escherichia coli Proteins
Flagella/metabolism
Genes, Bacterial
Genetic Complementation Test
Membrane Proteins
Molecular Sequence Data
Mutation/genetics
Operon/genetics
Plasmids/genetics
Protein Sorting Signals/genetics
Recombinant Fusion Proteins/genetics,metabolism
Chemicals
Bacterial Proteins
Escherichia coli Proteins
FliQ protein, E coli
Membrane Proteins
Protein Sorting Signals
Recombinant Fusion Proteins
FliP protein, Bacillus
fliZ protein, Bacillus subtilis
FliQ protein, Bacteria
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bischoff D S
Department of Biochemistry, College of Medicine, University of Illinois, Urbana 61820.
Weinreich M D
Ordal G W
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