Urease-associated heat shock protein of Helicobacter pylori

Infect Immun. 1992 May;60(5):2125-7. doi: 10.1128/iai.60.5.2125-2127.1992.

Abstract

Helicobacter pylori urease is an extracellular, cell-bound enzyme with a molecular weight of approximately 600,000 (600K enzyme) comprising six 66K and six 31K subunits. A 62K protein is closely associated with the H. pylori urease, both in crude preparations and after gel filtration; this protein can be removed from the urease by ion-exchange chromatography without inactivating the enzyme. We purified this urease-associated protein and determined its N-terminal amino acid sequence. The sequence is 80% homologous (identical plus conserved amino acid residues) to the Escherichia coli GroEL heat shock protein (HSP), 75% homologous to the human homolog, and 84% homologous to the HSP homolog found in species of Chlamydia. Thus, the 62K urease-associated protein of H. pylori belongs to the HSP60 family of stress proteins known as chaperonins. Evidently this protein, HSP62, participates in the extracellular assembly and/or protection of the urease against inactivation in the hostile environment of the stomach.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / analysis
  • Chaperonin 60
  • Heat-Shock Proteins / analysis*
  • Heat-Shock Proteins / immunology
  • Heat-Shock Proteins / physiology
  • Helicobacter pylori / chemistry*
  • Molecular Sequence Data
  • Urease / analysis*

Substances

  • Bacterial Proteins
  • Chaperonin 60
  • Heat-Shock Proteins
  • Urease