A chaperone with a hydrophilic surface.
The folding of native tubulin involves at least seven different chaperone proteins: prefoldin, the cytosolic chaperonin CCT and five tubulin-specific chaperone proteins named cofactors A-E. The structure of the yeast homolog of cofactor A, Rbl2p, shows it to be a dimer with largely hydrophilic surfaces, reflecting the fact that it interacts with quasi-native, not unfolded, beta-tubulin.
Cowan
N J
NJ
Department of Biochemistry, New York University Medical Center, 550 First Avenue, New York, New York 10016, USA. cowann01@mcrcr.med.nyu.edu
Lewis
S A
SA
D000818:Animals; D008869:Microtubule-Associated Proteins / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism*; D055672:Static Electricity; D014404:Tubulin / Q000737:chemistry* / Q000378:metabolism*
D008869:Microtubule-Associated Proteins; D018832:Molecular Chaperones; C443671:RBL2 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014404:Tubulin