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© The Rockefeller University Press, 0021-9525/1999//265 $5.00
The Journal of Cell Biology, Volume 145, Number 2, , 1999 265-277

Prefoldin–Nascent Chain Complexes in the Folding of Cytoskeletal Proteins

William J. Hansen^*, Nicholas J. Cowan, and William J. Welch^*

^* Surgical Research Laboratory, San Francisco General Hospital, Departments of Surgery, Medicine, and Physiology, University of California, San Francisco, California 94143; and Department of Biochemistry, New York University School of Medicine, New York, New York 10016

In vitro transcription/translation of actin cDNA and analysis of the translation products by native-PAGE was used to study the maturation pathway of actin. During the course of actin synthesis, several distinct actin-containing species were observed and the composition of each determined by immunological procedures. After synthesis of the first 145 amino acids, the nascent ribosome-associated actin chain binds to the recently identified heteromeric chaperone protein, prefoldin (PFD). PFD remains bound to the relatively unfolded actin polypeptide until its posttranslational delivery to cytosolic chaperonin (CCT). We show that - and β-tubulin follow a similar maturation pathway, but to date find no evidence for an interaction between PFD and several noncytoskeletal proteins. We conclude that PFD functions by selectively targeting nascent actin and tubulin chains pending their transfer to CCT for final folding and/or assembly.

Key Words: protein folding • molecular chaperones • cytoskeletal proteins • protein synthesis • actin • tubulin

Abbreviations used in this paper: 7-^MeGMP, 7-methylguanosine monophosphate; CCT, cytosolic chaperonin; PFD, prefoldin.

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