In vivo observation of polypeptide flux through the bacterial chaperonin system
Article Abstract:
Researchers have investigated the flux of newly synthesized proteins through chaperonin GroEL in living E. coli cells and upon cell-free translation. It was established that only between 10% and 15% of all newly synthesized polypeptide chains interact with GroEL under nonstress conditions and transit the chaperonin extremely quickly. The extent to which the population of a particular protein interacts with GroEL in vivo is usually determined by its rate of folding, the cellular GroEL concentration and the affinity of its folding intermediates for GroEL.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
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Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent
Article Abstract:
A study of the crystal structure of an Hsp90-geldanamycin complex was conducted. The structure of the geldanamycin-binding domain of Hsp90 shows a pocket. When geldanamycin binds inside this pocket, a compact structure similar to that of a polypeptide chain in a turn conformation is adopted. The findings suggest that the pocket binds a part of the polypeptide substrate and is involved in the conformational maturation/refolding reaction.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
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A stress sensor for the bacterial periplasm
Article Abstract:
The stress response in bacteria, consisting of stress sensing and reaction in the periplasm is independent of the one found in cytoplasm. The activation of bacterial periplasmic stress sensor DegS is mediated by releasing the inhibition of its protease domain initiating a proteolysis cascade that leads to the synthesis of periplasmic chaperone proteins.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2003
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