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. 2002 Jun;184(11):2925–2930. doi: 10.1128/JB.184.11.2925-2930.2002

FIG. 1.

FIG. 1.

Structural organization of H. pylori chaperone genes (17, 21). Grey arrow bars indicate chaperone genes, black arrow bars indicate regulatory genes (hspR and hrcA), and the white arrow bar indicates a putative helicase-like gene. Chaperone genes groES and groEL code for the HspA (Hsp10) and HspB (Hsp60) proteins (20); cbpA encodes a protein with 30% amino acid identity (in a 288-amino-acid overlap) to the cochaperone curved DNA binding protein CbpA from E. coli, a homologue of DnaJ (22); hspR encodes a regulatory protein with 46% identity (in a 91-amino-acid overlap) to HspR, the negative regulator of heat shock genes in S. coelicolor (2); the helicase-like open reading frame encodes a protein with 30% identity within 421 amino acids to a hypothetical helicase-like protein from Haemophilus influenzae; hrcA encodes a protein with 28% identity (in a 71-amino-acid overlap) to the heat-inducible transcriptional repressor HrcA from B. subtilis (23); and grpE and dnaK encode the GrpE and DnaK (Hsp70) chaperones, respectively.