Affiliation:
1. Nagasaki University School of Dentistry, Nagasaki City, Japan.
Abstract
A novel 18-kDa heat shock protein, HrpA, has been identified from Mycobacterium bovis BCG. HrpA was rapidly synthesized in membrane and ribosome fractions but not in the cytoplasmic fraction under heat shock stress. HrpA bound tightly to 70S ribosomes, mainly in 30S subunits. HrpA might be involved in the initiation step of translation at high temperature.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference15 articles.
1. Induction of mycobacterial proteins during phagocytosis and heat shock: a time interval analysis;Alavi M. R.;J. Leukocyte Biol.,1994
2. Detachment of ribosomal proteins by salt. II. Some properties of protein-deficient particles formed by the attachment of ribosomal proteins;Atsmon A.;J. Mol. Biol.,1969
3. Structure of LiCl core particles of 50S ribosomal subunits from Escherichia coli by electron microscopy;Boublik M.;Cytobiologie,1978
4. Suppression of a cold-sensitive mutation in 16S rRNA by overexpression of a novel ribosome-binding factor;Dammel C. S.;RbfA. Genes Dev.,1995
5. Variation in protection by BCG: implications of and for heterologous immunity;Fine P. E. M.;Lancet,1995
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