The purification of a GroEL-like stress protein from aerobically adapted Campylobacter jejuni.
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.
Takata
T
T
Department of Clinical Chemistry and Laboratory Medicine, Faculty of Medicine, Fukuoka University, Japan.
Wai
S N
SN
Takade
A
A
Sawae
Y
Y
Ono
J
J
Amako
K
K
D000222:Adaptation, Physiological; D000332:Aerobiosis; D000595:Amino Acid Sequence; D001431:Bacteriological Techniques; D016123:Campylobacter jejuni / Q000737:chemistry / Q000502:physiology* / Q000648:ultrastructure; D018834:Chaperonin 60 / Q000737:chemistry / Q000302:isolation & purification*; D002692:Chlamydia trachomatis / Q000737:chemistry; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000302:isolation & purification; D016480:Helicobacter pylori / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017386:Sequence Homology, Amino Acid; D013314:Stress, Mechanical
D018834:Chaperonin 60; D006360:Heat-Shock Proteins