Construction and analyses of mutant ftsH alleles of Bacillus subtilis involving the ATPase- and Zn-binding domains.

doi:10.1007/s00284-004-4319-2

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Article

Construction and analyses of mutant ftsH alleles of Bacillus subtilis involving the ATPase- and Zn-binding domains.

Current microbiology - 1 Sept 2004

Kotschwar Matthias, Harfst Evita, Ohanjan Tanja, Schumann Wolfgang

Abstract excerpt

The ftsH gene, present in all eubacterial species, is anchored in the cytoplasmic membrane and contains an ATP- and a Zn-binding domain that are both part of a metalloprotease activity. The Bacillus subtilis ftsH is not essential, but null mutants exhibit a pleiotropic phenotype including filamentous growth; hypersensitivity towards heat and salt stress and a failure to sporulate. To find out whether one or the...

Topics

Adenosine Triphosphatases
Alleles
Bacillus subtilis
Bacterial Proteins
Binding Sites
Caseins
Genes, Bacterial
Membrane Proteins
Phenotype
Point Mutation
Protein Structure, Tertiary
Recombinant Fusion Proteins
Subtilisin
Zinc

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Identifiers

PMID: 15386101
DOI: 10.1007/s00284-004-4319-2

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