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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 :-
FxxxI/LxxEHGI
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.
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References:-
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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