Proceedings of the National Academy of Sciences • Vol 91 • No 7
Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta.
March 1994 • David Miklos, Shari L. Caplan, D.R. Mertens, Gavin Hynes, Zachary W. Pitluk, Yechezkel Kashi, Kimberly Harrison-Lavoie, Stevenson G. S, C. Randell Br…
A role for heterooligomeric TCP1 complex as a chaperonin in the eukaryotic cytosol has recently been suggested both by structural similarities with other chaperonins and by in vitro experiments showing it to mediate ATP-dependent folding of actin, tubulin, and luciferase. Here we present the primary structure of a second subunit of the complex and present genetic and functional analyses. The TCP1 beta amino acid sequence, predicted from the cloned gene, bears 35% identity to TCP1, termed here TCP1 alpha, containin…