title: [Properties of thermostable HtpR-mutant of Escherichia coli].
abstract: A thermoresistant htpR mutant having a decreased level of proteolytic activity has been selected in E. coli strain K802 after the directed mutagenesis in vivo. The mutation results in the bacteriophage T7 RNA-polymerase stability, aminoglycosidephosphotransferase stability as well as in the decrease in the rate of proteolytic degradation of cytoplasmic proteins during the heat shock. The obtained mutant strain can, probably be used as a host for alien polypeptides production.
authors.forename: V I
authors.initials: VI
authors.lastname: Kiselev
authors.forename: I M
authors.initials: IM
authors.lastname: Tarasova
authors.forename: A Iu
authors.initials: AIu
authors.lastname: Malinin
authors.forename: O I
authors.initials: OI
authors.lastname: Kiselev
authors.forename: A I
authors.initials: AI
authors.lastname: Glukhov
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D005798:Genes, Bacterial; D006358:Hot Temperature; D006868:Hydrolysis; D009154:Mutation; D010957:Plasmids
chemical_list: D000255:Adenosine Triphosphate
vernacular_title: Svoĭstva termoustoĭchivogo HtpR-mutanta Escherichia coli.