RRC ID 15626
著者 Sugimoto S, Saruwatari K, Higashi C, Tsuruno K, Matsumoto S, Nakayama J, Sonomoto K.
タイトル In vivo and in vitro complementation study comparing the function of DnaK chaperone systems from halophilic lactic acid bacterium Tetragenococcus halophilus and Escherichia coli.
ジャーナル Biosci Biotechnol Biochem
Abstract In this study, we characterized the DnaK chaperone system from Tetragenococcus halophilus, a halophilic lactic acid bacterium. An in vivo complementation test showed that under heat stress conditions, T. halophilus DnaK did not rescue the growth of the Escherichia coli dnaK deletion mutant, whereas T. halophilus DnaJ and GrpE complemented the corresponding mutations of E. coli. Purified T. halophilus DnaK showed intrinsic weak ATPase activity and holding chaperone activity in vitro, but T. halophilus DnaK did not cooperate with the purified DnaJ and GrpE from either T. halophilus or E. coli in ATP hydrolysis or luciferase-refolding reactions under the conditions tested. E. coli DnaK, however, cross-reacted with those from both bacteria. This difference in the cooperation with DnaJ and GrpE appears to result in an inability of T. halophilus DnaK to replace the in vivo function of the DnaK chaperone of E. coli.
巻・号 72(3)
ページ 811-22
公開日 2008-3-1
DOI 10.1271/bbb.70691
PII JST.JSTAGE/bbb/70691
PMID 18323638
MeSH Bacterial Proteins / genetics Bacterial Proteins / physiology* Escherichia coli Proteins / genetics Escherichia coli Proteins / physiology* Genetic Complementation Test HSP40 Heat-Shock Proteins / genetics HSP40 Heat-Shock Proteins / physiology HSP70 Heat-Shock Proteins / genetics HSP70 Heat-Shock Proteins / physiology Heat Stress Disorders Lactobacillus / chemistry* Molecular Chaperones* Mutation
IF 1.516
引用数 11
WOS 分野 FOOD SCIENCE & TECHNOLOGY CHEMISTRY, APPLIED BIOTECHNOLOGY & APPLIED MICROBIOLOGY BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
一般微生物 JCM 5888