A novel dnaK operon from Porphyromonas gingivalis

FEBS Letters

Yamashita, Yoshihisa²  Ohishi, Masamichi¹  Koga, Toshihiko²  Yoshida, Akihiro¹  Nakano, Yoshio²  Shibata, Yukie²  Oho, Takahiko² 

[1] First Department of Oral and Maxillofacial Surgery, Faculty of Dentistry, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan;Department of Preventive Dentistry, Faculty of Dentistry, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan

关键词: dnaK operon;    Heat shock protein;    Molecular chaperone;    Small heat shock protein;    Porphyromonas gingivalis;    aa;    amino acid(s);    IPTG;    isopropyl-β-d-thiogalactopyranoside;    ORF;    open reading frame;    PCR;    polymerase chain reaction;    RT-PCR;    reverse transcriptase-mediated PCR;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(99)00237-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The nucleotide sequence of the dnaK operon cloned from Porphyromonas gingivalis revealed that the operon does not contain homologues of either dnaJ or grpE. However, there were two genes which encode small heat shock proteins immediately downstream from the dnaK and they were transcribed together with dnaK as one unit. The ATPase activity of the P. gingivalis DnaK was synergistically stimulated up to 40-fold in the simultaneous presence of Escherichia coli DnaJ and GrpE. These results suggest that the DnaK homologue of P. gingivalis, with its unique genetic structure and evolutionary features, works as a member of the DnaK chaperone system.

【 授权许可】

Unknown