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

Yasuhiro Tabira; Naoya Ohara; Takeshi Yamada

doi:10.1006/mpat.2000.0384

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

Yasuhiro Tabira, Naoya Ohara, Takeshi Yamada

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	213-222
Number of pages	10
Journal	Microbial Pathogenesis
Volume	29
Issue number	4
DOIs	https://doi.org/10.1006/mpat.2000.0384
Publication status	Published - 2000
Externally published	Yes

Keywords

BCG
HSP
Heat stress
Molecular chaperone
Oxydative stress

ASJC Scopus subject areas

Microbiology
Infectious Diseases

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1006/mpat.2000.0384

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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.",

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AU - Tabira, Yasuhiro

AU - Ohara, Naoya

AU - Yamada, Takeshi

PY - 2000

Y1 - 2000

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AB - 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.

KW - BCG

KW - HSP

KW - Heat stress

KW - Molecular chaperone

KW - Oxydative stress

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

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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