Hilfe Wegweiser Datenschutzhinweis Impressum Kontakt





Group II chaperonins: new TRiC(k)s and turns of a protein folding machine

Es sind keine MPG-Autoren in der Publikation vorhanden
Externe Ressourcen
Es sind keine Externen Ressourcen verfügbar
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar

Gutsche, I., Essen, L. O., & Baumeister, W. (1999). Group II chaperonins: new TRiC(k)s and turns of a protein folding machine. Journal of Molecular Biology., 293(2), 295-312.

In the past decade, the eubacterial group I chaperonin GroEL became the paradigm of a protein folding machine. More recently, electron microscopy and X-ray crystallography offered insights into the structure of the thermosome, the archetype of the group II chaperonins which also comprise the chaperonin from the eukaryotic cytosol TRiC. Some structural differences from GroEL were revealed, namely the existence of a built-in lid provided by the helical protrusions of the apical domains instead of a GroES-like co-chaperonin. These structural studies provide a framework for understanding the differences in the mode of action between the group II and the group I chaperonins. In vitro analyses of the folding of non-native substrates coupled to ATP binding and hydrolysis are progressing towards establishing a functional cycle for group II chaperonins. A protein complex called GimC/prefoldin has recently been found to cooperate with TRiC in vivo, and its characterization is under way. Copyright 1999 Academic Press. [References: 109]