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  • Title: A single amino acid residue is responsible for species-specific incompatibility between CCT and alpha-actin.
    Author: Altschuler GM, Dekker C, McCormack EA, Morris EP, Klug DR, Willison KR.
    Journal: FEBS Lett; 2009 Feb 18; 583(4):782-6. PubMed ID: 19183552.
    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.
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