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The Purification of a GroEL‐Like Stress Protein from Aerobically Adapted Campylobacter jejuni
Author(s) -
Takata Tohru,
Wai Sun Nyunt,
Takade Akemi,
Sawae Yoshiro,
Ono Junko,
Amako Kazunobu
Publication year - 1995
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1995.tb03245.x
Subject(s) - groel , campylobacter jejuni , biology , heat shock protein , hsp60 , groes , microbiology and biotechnology , antiserum , yersinia enterocolitica , campylobacter fetus , escherichia coli , campylobacter coli , campylobacter , chlamydia trachomatis , yersinia , size exclusion chromatography , biochemistry , bacteria , hsp70 , antibody , gene , genetics , virology , enzyme
From plate cultures of Campylobacter jejuni grown in room air a particulate protein of 62 kDa was isolated by ion‐exchange chromatography. The protein had a square shape from the side view but when viewed from the top it had a star‐shaped structure. The molecular size of the whole particle determined by gel filtration was 850 kDa which suggested the presence of 14 subunits of 62 kDa in each particle. The N‐terminal 37 amino residues showed more than 80% homology with the sequence of these heat shock protein (HSP) 60 homologs of Chlamydia trachomatis, Helicobacter pylori , and Escherichia coli (GroEL). This protein is immunologically cross‐reactive with the antiserum for the 60‐kDa HSP of Yersinia enterocolitica . Production of the 62‐kDa protein increased under heat stress and growth in an aerobic atmospheric environment. From these observations we concluded that the 62‐kDa protein is a Campylobacter stress protein (Cj62) which belongs to the HSP 60 family.