TY - JOUR
T1 - In vivo and in vitro complementation study comparing the function of DnaK chaperone systems from halophilic lactic acid bacterium Tetragenococcus halophilus and Escherichia coli
AU - Sugimoto, Shinya
AU - Saruwatari, Kozue
AU - Higashi, Chihana
AU - Tsuruno, Keigo
AU - Matsumoto, Shunsuke
AU - Nakayama, Jiro
AU - Sonomoto, Kenji
N1 - Funding Information:
We thank Dr. Teru Ogura (Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Japan) for providing E. coli dnaJ mutant (AR7059), and Dr. Costa Georgopoulos (Département de Microbiologie et Médecine Moléculaire, Centre Médical Universitaire, Switzerland) for sending us E. coli grpE mutant (DA259). This work was supported in part by a grant from the JSPS Research Fellowship (0166799) for young scientists.
PY - 2008
Y1 - 2008
N2 - 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.
AB - 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.
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U2 - 10.1271/bbb.70691
DO - 10.1271/bbb.70691
M3 - Article
C2 - 18323638
AN - SCOPUS:41549164027
SN - 0916-8451
VL - 72
SP - 811
EP - 822
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 3
ER -