Identification and characterization of the ribosome-associated protein, HrpA, of Bacillus Calmette-Guerin

Yasuhiro Tabira, Naoya Oohara, Takeshi Yamada

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

HrpA was found as a ribosome-associated protein which appeared in heat-stressed Mycobacterium bovis Bacillus Calmette-Guerin. Here, we have studied the function of HrpA in vitro. HrpA is a heat shock protein belonging to a small heat shock protein family. The putative molecular mass was 17784.86 kDa. Recombinant HrpA formed large complexes of nonamer or dodecamer. HrpA prevented the aggregation of enzymes under heat shock conditions, and it formed stable complexes with partially denatured enzymes. HrpA was induced temporarily by oxygen repletion after anaerobic condition. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)213-222
Number of pages10
JournalMicrobial Pathogenesis
Volume29
Issue number4
DOIs
Publication statusPublished - 2000
Externally publishedYes

Fingerprint

Mycobacterium bovis
Ribosomes
Hot Temperature
Small Heat-Shock Proteins
Enzymes
Heat-Shock Proteins
Shock
Proteins
Oxygen
In Vitro Techniques

Keywords

  • BCG
  • Heat stress
  • HSP
  • Molecular chaperone
  • Oxydative stress

ASJC Scopus subject areas

  • Microbiology
  • Infectious Diseases

Cite this

Identification and characterization of the ribosome-associated protein, HrpA, of Bacillus Calmette-Guerin. / Tabira, Yasuhiro; Oohara, Naoya; Yamada, Takeshi.

In: Microbial Pathogenesis, Vol. 29, No. 4, 2000, p. 213-222.

Research output: Contribution to journalArticle

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