The ClpB ATPase of Streptomyces albus G belongs to the HspR heat shock regulon
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چکیده
منابع مشابه
Characterization of Streptomyces albus 18-kilodalton heat shock-responsive protein.
In Streptomyces albus during the heat shock response, a small heat shock protein of 18 kDa is dramatically induced. This protein was purified, and internal sequences revealed that S. albus HSP18 showed a marked homology with proteins belonging to the family of small heat shock proteins. The corresponding gene was isolated and sequenced. DNA sequence analysis confirmed that the hsp18 gene produc...
متن کاملThe RheA repressor is the thermosensor of the HSP18 heat shock response in Streptomyces albus.
Microorganisms have mechanisms to sense their environment and rapidly adapt to survive changes in conditions. In Streptomyces albus, various transcriptional repressors mediate the induction of heat shock genes. The RheA repressor regulates the synthesis of HSP18, a small heat shock protein, which plays a role in thermotolerance. The RheA protein was purified to determine how it responds rapidly...
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The exoceilular f-lactamase of Streptomyces albus G has been purified to near protein homogeneity. It consists of one single polypeptide chain of mol.wt. 30000-31000, has a rather low isoelectric point (at pH 6.0) and contains less lysine (2.1%) and more half-cystine residues than most fi-lactamases from other Gram-positive bacteria. Penicillins are much better substrates than A3-cephalosporins...
متن کاملThe active sites of the beta-lactamases of Streptomyces cacaoi and Streptomyces albus G.
The active-site serine of the extracellular beta-lactamases of Streptomyces cacaoi and Streptomyces albus G has been labelled with beta-iodopenicillanate. The determination of the sequence of the labelled peptides obtained after trypsin digestion of the denatured proteins indicate both enzymes to be class A beta-lactamases. Surprisingly the two Streptomyces enzymes do not appear to be especiall...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 1999
ISSN: 0950-382X,1365-2958
DOI: 10.1046/j.1365-2958.1999.01193.x