SGD Paper 
Altschuler GM, et al. (2009) A single amino acid residue is responsible for species-specific incompatibility between CCT and alpha-actin. FEBS Lett 583(4):782-6
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 (beta/gamma) actins but is now found to be incapable of folding mammalian skeletal muscle alpha-actin. Arrest of alpha-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 alpha-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.
| Status: Published | Type: Journal Article | PubMed ID: 19183552 |
Topics addressed in this paper
Number of different genes curated to this paper: 10
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