Prefoldin-Nascent Chain Complexes in the Folding of Cytoskeletal Proteins

doi:10.1083/jcb.145.2.265

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J. Cell Biol., Volume 145, Number 2, April 19, 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 studythe maturation pathway of actin. During the course of actin synthesis,several distinct actin-containing species were observed and thecomposition of each determined by immunological procedures. Aftersynthesis of the first ~145 amino acids, the nascent ribosome-associatedactin chain binds to the recently identified heteromeric chaperoneprotein, prefoldin (PFD). PFD remains bound to the relativelyunfolded actin polypeptide until its posttranslational deliveryto cytosolic chaperonin (CCT). We show that $alpha$ - and $beta$ -tubulin followa similar maturation pathway, but to date find no evidence foran interaction between PFD and several noncytoskeletal proteins.We conclude that PFD functions by selectively targeting nascentactin and tubulin chains pending their transfer to CCT for finalfolding and/orassembly.

Key words: protein folding; molecular chaperones; cytoskeletal proteins; protein synthesis; actin; tubulin

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