Co-evolution-driven switch of J-protein specificity towards an Hsp70 partner.
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.
Department of Molecular and Cellular Biology, Faculty of Biotechnology, University of Gdansk, Gdansk, Poland.
Sebastian
S
Pukszta
Brenda
B
Schilke
Rafal
R
Dutkiewicz
Jacek
J
Kominek
Kaja
K
Moczulska
Barbara
B
Stepien
Krista G
KG
Reitenga
Janusz M
JM
Bujnicki
Barry
B
Williams
Elizabeth A
EA
Craig
Jaroslaw
J
Marszalek
D000595:Amino Acid Sequence; D019143:Evolution, Molecular; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D008957:Models, Genetic; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*
D018840:HSP70 Heat-Shock Proteins; C115914:JAC1 protein, S cerevisiae; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins