Co-evolution-driven switch of J-protein specificity towards an Hsp70 partner.
EMBO Rep
; 11(5): 360-5, 2010 May.
Article
em En
| MEDLINE
| ID: mdl-20224575
ABSTRACT
Molecular mechanisms by which protein-protein interactions are preserved or lost after gene duplication are not understood. Taking advantage of the well-studied yeast mtHsp70J-protein molecular chaperone system, we considered whether changes in partner proteins accompanied specialization of gene duplicates. Here, we report that existence of the Hsp70 Ssq1, which arose by duplication of the gene encoding multifunction mtHsp70 and specializes in iron-sulphur cluster biogenesis, correlates with functional and structural changes in the J domain of its J-protein partner Jac1. All species encoding this shorter alternative version of the J domain share a common ancestry, suggesting that all short JAC1 proteins arose from a single deletion event. Construction of a variant that extended the length of the J domain of a 'short' Jac1 enhanced its ability to partner with multifunctional Hsp70. Our data provide a causal link between changes in the J protein partner and specialization of duplicate Hsp70.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
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Chaperonas Moleculares
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Proteínas de Choque Térmico HSP70
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Evolução Molecular
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Proteínas de Saccharomyces cerevisiae
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article