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Co‐evolution‐driven switch of J‐protein specificity towards an Hsp70 partner
Author(s) -
Pukszta Sebastian,
Schilke Brenda,
Dutkiewicz Rafal,
Kominek Jacek,
Moczulska Kaja,
Stepien Barbara,
Reitenga Krista G,
Bujnicki Janusz M,
Williams Barry,
Craig Elizabeth A,
Marszalek Jaroslaw
Publication year - 2010
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2010.29
Subject(s) - biogenesis , gene duplication , biology , gene , hsp70 , genetics , chaperone (clinical) , protein domain , computational biology , heat shock protein , microbiology and biotechnology , medicine , pathology
Molecular mechanisms by which protein–protein interactions are preserved or lost after gene duplication are not understood. Taking advantage of the well–studied yeast mtHsp70:J–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.