Cloning and nucleotide sequence analysis of immunodominant heat-shock protein of Yersinia enterocolitica.
Yersinia enterocolitica, a highly antigenic 60-kDa protein, designated cross-reacting protein antigen (CRPA), is a member of the chaperonin-60 family of molecular chaperones. The gene encoding CRPA was cloned, expressed and sequenced. A partial library from Y. enterocolitica 0:3 genomic DNA was constructed in vector pUC19 and was screened by the immunoreactivity to monoclonal antibody 1A4, which has specificity for a species-specific epitope on the CRPA molecule. The crpA gene region consists of a putative two-cistron operon encoding proteins of 549 and 97 amino acids. The operon structure was led by a consensus heat-shock promoter sequence. Homology searches using the derived amino acid sequence have revealed that CRPA is 88.2% identical to GroEL of Escherichia coli. CRPB, another protein encoded by the operon, shows extensive sequence homology, 91.8% identical to GroES of E. coli which is a member of chaperonin-10.
Yamamoto
T
T
Department of Microbiology, Kyorin University School of Medicine, Tokyo.
Miura
H
H
Ohsumi
K
K
Yamaguchi
H
H
Taguchi
H
H
Ogata
S
S
D001483:Base Sequence / Q000235:genetics; D015139:Blotting, Southern; D015153:Blotting, Western; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics*; D005798:Genes, Bacterial / Q000235:genetics*; D006360:Heat-Shock Proteins / Q000235:genetics*; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D009876:Operon / Q000235:genetics; D015008:Yersinia enterocolitica / Q000235:genetics*
D004269:DNA, Bacterial; D006360:Heat-Shock Proteins