The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage
The molecular chaperones Hsp70 and Hsp90 participate in many important cellular processes, including how cells respond to DNA damage. Here we show the results of applied quantitative affinity-purification mass spectrometry (AP-MS) proteomics to understand the protein network through which Hsp70 and...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2015-03-01
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| Series: | Data in Brief |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340914000249 |
| _version_ | 1819108520635662336 |
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| author | Andrew W. Truman Kolbrun Kristjansdottir Donald Wolfgeher Natalia Ricco Anoop Mayampurath Samuel L. Volchenboum Josep Clotet Stephen J. Kron |
| author_facet | Andrew W. Truman Kolbrun Kristjansdottir Donald Wolfgeher Natalia Ricco Anoop Mayampurath Samuel L. Volchenboum Josep Clotet Stephen J. Kron |
| author_sort | Andrew W. Truman |
| collection | DOAJ |
| description | The molecular chaperones Hsp70 and Hsp90 participate in many important cellular processes, including how cells respond to DNA damage. 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. (2013) [2]) with the dataset identifier PXD001284. |
| first_indexed | 2024-12-22T03:11:14Z |
| format | Article |
| id | doaj.art-63269709f24d4572a2a4ed3c4dae6cd4 |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-12-22T03:11:14Z |
| publishDate | 2015-03-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-63269709f24d4572a2a4ed3c4dae6cd42022-12-21T18:40:55ZengElsevierData in Brief2352-34092015-03-012C121510.1016/j.dib.2014.10.006The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damageAndrew W. Truman0Kolbrun Kristjansdottir1Donald Wolfgeher2Natalia Ricco3Anoop Mayampurath4Samuel L. Volchenboum5Josep Clotet6Stephen J. Kron7Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USADepartment of Biomedical Sciences, Midwestern University, Downers Grove, IL 60515, USADepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USADepartament de Ciències Bàsiques, Universitat Internacional de Catalunya, Barcelona, Catalunya, SpainComputation Institute, The University of Chicago, Chicago, IL 60637, USAComputation Institute, The University of Chicago, Chicago, IL 60637, USADepartament de Ciències Bàsiques, Universitat Internacional de Catalunya, Barcelona, Catalunya, SpainDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USAThe molecular chaperones Hsp70 and Hsp90 participate in many important cellular processes, including how cells respond to DNA damage. 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. (2013) [2]) with the dataset identifier PXD001284.http://www.sciencedirect.com/science/article/pii/S2352340914000249 |
| spellingShingle | Andrew W. Truman Kolbrun Kristjansdottir Donald Wolfgeher Natalia Ricco Anoop Mayampurath Samuel L. Volchenboum Josep Clotet Stephen J. Kron The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage Data in Brief |
| title | The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage |
| title_full | The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage |
| title_fullStr | The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage |
| title_full_unstemmed | The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage |
| title_short | The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage |
| title_sort | quantitative changes in the yeast hsp70 and hsp90 interactomes upon dna damage |
| url | http://www.sciencedirect.com/science/article/pii/S2352340914000249 |
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