Cytosolic chaperonins: a question of promiscuity.
Chaperonins in the eukaryotic cytosol are more mysterious than their bacterial counterparts, with a heterogeneity of protein binding surfaces. In a recent issue of Molecular Cell, showed that binding specificity in the TRiC chaperonin is less than absolute and resolved the location of substrate binding surfaces in this chaperonin.
Clarke
Anthony R
AR
Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom.
D000251:Adenosine Triphosphatases / Q000737:chemistry; D019843:Archaeal Proteins / Q000378:metabolism; D001665:Binding Sites; D018834:Chaperonin 60 / Q000737:chemistry; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins / Q000378:metabolism / Q000502:physiology*; D003593:Cytoplasm / Q000378:metabolism; D003600:Cytosol / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D008954:Models, Biological; D018832:Molecular Chaperones; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding
D019843:Archaeal Proteins; D018834:Chaperonin 60; D018832:Molecular Chaperones; D000251:Adenosine Triphosphatases; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins