A single amino acid residue is responsible for species-specific incompatibility between CCT and α-actin |
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Authors: | G.M. Altschuler C. Dekker E.P. Morris K.R. Willison |
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Affiliation: | a Section of Cell and Molecular Biology, Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, United Kingdom b Section of Structural Biology, Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, United Kingdom c Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, United Kingdom |
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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. |
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Keywords: | Actin ACT1 Muscle CCT Chaperonin Protein folding |
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