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A chaperone protein that appear to recognise similar motifs on both b-actin and a-tubulin (Rommelaere et al, 2001). Prefoldin binds unfolded actin so in this limited sense it is an actin-binding protein. The motif is :-


This motif is present at the N-terminus of both actin and tubulin.  Prefoldin binds to the nascent chain of actin as it is being translated.  It seems to bind the first 145 amino-acids (Hanson et al, 1999), including the suggested motif (Rommelaere et al, 2001).  Prefoldin remains bound to the unfolded actin and passes it on to the CCT chaperonin complex which further folds the protein. 



Hansen, W. J., Cowan, N. J. & Welch, W. J. (1999) Prefoldin-Nascent Chain Complexes in the Folding of Cytoskeletal Proteins. J. Cell Biol. 145, 265-277.

Rommelaere, H., De Neve, M., Neirynck, K., Peelaers, D., Waterschoot, D., Goethals, M., Fraeyman, N., Vandekerckhove, J. & Ampe, C. (2001) Prefoldin recognition motifs in the nonhomologous proteins of the actin and tubulin families. J. Biol.Chem. 276, 41023-41028.

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