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Functional role of a consensus peptide which is common to α‐, β‐, and γ‐tubulin, to actin and centractin, to phytochrome A, and to the TCP1α chaperonin protein
Author(s) -
Burns Roy G.,
Surridge Christopher D.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00522-2
Subject(s) - peptide , chaperonin , actin , biology , tubulin , phytochrome , cytoskeleton , microbiology and biotechnology , gene isoform , biochemistry , peptide sequence , protein folding , microtubule , gene , botany , red light , cell
The TRiC (TCP1 Ring Complex) chaperonin complex participates in the functional folding of actin, centractin, α‐,β‐,γ‐tubulin, and phytochrome. Each of the cytoskeletal proteins contain a peptide, RK(A,C,T)F/KRAF, located towards the C‐terminus, which is homologous to a TCP1α peptide, while the equivalent phytochrome peptide (RLKAF in certain isoforms) is very similar to the KLRAF peptide of TCP1α. We propose that this TCP1α peptide binds to the nascent polypeptides as they emerge from the ribosome, that this binding restricts the folding pathway, and that the TCP1α peptide is subsequently displaced by the synthesis of the consensus peptide. This hypothesis is strongly supported by the crystallographic structure of actin.