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A chaperone with a hydrophilic surface

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Abstract

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, β-tubulin.

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Figure 1: Tubulin folding pathway.

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Authors and Affiliations

  1. the Department of Biochemistry, New York University Medical Center, 550 First Avenue, New York, 10016, New York, USA

    Nicholas J. Cowan & Sally A. Lewis

Authors
  1. Nicholas J. Cowan
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  2. Sally A. Lewis
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Correspondence to Nicholas J. Cowan.

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Cowan, N., Lewis, S. A chaperone with a hydrophilic surface. Nat Struct Mol Biol 6, 990–991 (1999). https://doi.org/10.1038/14870

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