A chaperone with a hydrophilic surface

The folding of native tubulin involves at least seven different chaperone p roteins: 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 surfa ces, reflecting the fact that it interacts with quasi-native, not unfolded, beta-tubulin.