Physiological consequences of mutations in the htpG heat shock gene of Escherichia coli.

doi:10.1016/j.mrfmmm.2013.04.003

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Article

Physiological consequences of mutations in the htpG heat shock gene of Escherichia coli.

Mutation research - 1 Jan 2000

Grudniak Anna M, Pawlak Katarzyna, Bartosik Katarzyna, Wolska Krystyna I

Abstract excerpt

Mutation of the heat shock gene, htpG, causes severe defects of several cellular functions in Escherichia coli. A null htpG mutant constructed by gene replacement was impaired in the biosynthesis and secretion of several enzymes, and in biofilm formation and proteolysis. A significant decrease in the activity of β-lactamase in the ΔhtpG mutant was observed at 42°C. The alkaline phosphatase activity in sonicates...

Topics

Alkaline Phosphatase
Biofilms
Canavanine
Escherichia coli
Escherichia coli Proteins
HSP90 Heat-Shock Proteins
Luminescent Measurements
Molecular Chaperones
Mutation
beta-Lactamases

Source

Open in PubMed

Identifiers

PMID: 23618614
DOI: 10.1016/j.mrfmmm.2013.04.003

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