The ins and outs of GroEL-mediated protein folding.
Two papers recently published in Cell investigate the role of protein encapsulation by GroEL in assisting folding. The first shows how encapsulation can "smooth" the folding landscape, accelerating folding of some proteins. The second defines a confinement-independent pathway, which allows GroEL to assist folding of substrates too large to be encapsulated.
Weissman
J S
JS
Howard Hughes Medical Institute, Department of Cellular and Molecular Pharmacology, University of California-San Francisco, San Francisco, CA 94143, USA.
D000255:Adenosine Triphosphate / Q000378:metabolism; D020134:Catalytic Domain; D018835:Chaperonin 10 / Q000378:metabolism; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism; D008024:Ligands; D008954:Models, Biological; D011487:Protein Conformation; D017510:Protein Folding; D012273:Ribulose-Bisphosphate Carboxylase
D018835:Chaperonin 10; D018834:Chaperonin 60; D008024:Ligands; D000255:Adenosine Triphosphate; D012273:Ribulose-Bisphosphate Carboxylase