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- Title
A single amino acid residue is responsible for species-specific incompatibility between CCT and α-actin
- Authors
Altschuler, G.M.; Dekker, C.; McCormack, E.A.; Morris, E.P.; Klug, D.R.; Willison, K.R.
- Abstract
Abstract: Actin is dependent on the type-II chaperonin CCT (chaperonin containing TCP-1) to reach its native state. In vitro, yeast CCT folds yeast and also mammalian cytoplasmic (β/γ) actins but is now found to be incapable of folding mammalian skeletal muscle α-actin. Arrest of α-actin on yeast CCT at a folding cycle intermediate has been observed by electron microscopy. This discovery explains previous observations in vivo that yeast mutants expressing only the muscle actin gene are non-viable. Mutational analysis identified a single specific α-actin residue, Asn-297, that confers this species/isoform folding specificity. The implications of this incompatibility for chaperonin mechanism and actin–CCT co-evolution are discussed.
- Subjects
MOLECULAR chaperones; PROTEIN folding; ACTIN; COEVOLUTION; GENETIC mutation; SPECIES specificity; PROTEIN genetics; GENE expression
- Publication
FEBS Letters, 2009, Vol 583, Issue 4, p782
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2009.01.031