Identification and characterization of the ribosome-associated protein, HrpA, of Bacillus Calmette-Guérin
| Autor: | Naoya Ohara, Yasuhiro Tabira, Takeshi Yamada |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Ribosomal Proteins
Molecular Sequence Data In Vitro Techniques Microbiology Ribosome law.invention DEAD-box RNA Helicases Bacterial Proteins law Heat shock protein Amino Acid Sequence Heat-Shock Proteins chemistry.chemical_classification Molecular mass biology Escherichia coli Proteins Binding protein Mycobacterium bovis Molecular biology Enzymes Molecular Weight Oxygen Infectious Diseases Dodecameric protein Enzyme chemistry Biochemistry Chaperone (protein) biology.protein Recombinant DNA Sequence Alignment Genome Bacterial RNA Helicases |
| Zdroj: | Microbial Pathogenesis. 29:213-222 |
| ISSN: | 0882-4010 |
| DOI: | 10.1006/mpat.2000.0384 |
| Popis: | HrpA was found as a ribosome-associated protein which appeared in heat-stressed Mycobacterium bovis Bacillus Calmette-Guérin. 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. |
| Databáze: | OpenAIRE |
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