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pmid:26217697
The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage.
Andrew W Truman · Kolbrun Kristjansdottir · Donald Wolfgeher · Natalia Ricco · Anoop Mayampurath · Samuel L Volchenboum · Josep Clotet · Stephen J Kron
Data in brief · 2015 doi:10.1016/j.dib.2014.10.006
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Experiment
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Complete file
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Here we show the results of applied quantitative affinity-purification mass spectrometry (AP-MS) proteomics to understand the protein network through which Hsp70 and Hsp90 exert their effects on the DNA damage response (DDR). We characterized the interactomes of the yeast Hsp70 isoform Ssa1 and Hsp90 isoform Hsp82 before and after exposure to methyl methanesulfonate. We identified 256 chaperone interactors, 146 of which are novel. Although the majority of chaperone interaction remained constant under DNA damage, 5 proteins (Coq5, Ast1, Cys3, Ydr210c and Rnr4) increased in interaction with Ssa1 and/or Hsp82. This data presented here are related to [1] (Truman et al., in press). The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository (Vizcaino et al. 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