Data for the identification of proteins and post-translational modifications of proteins associated to histones H3 and H4 in S. cerevisiae, using tandem affinity purification coupled with mass spectrometry

Data for the identification of proteins and post-translational modifications of proteins associated to histones H3 and H4 in S. cerevisiae, using tandem affinity purification coupled with mass spectrometry

Tandem affinity purification method (TAP) allows the efficient purification of native protein complexes which incorporate a target protein fused with the TAP tag. Purified multiprotein complexes can then be subjected to diverse types of proteomic analyses. Here we describe the data acquired after ap...

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Main Authors: M Luz Valero, Ramon Sendra, Mercè Pamblanco
Format: Article
Language:English
Published: Elsevier 2016-03-01
Series:Data in Brief
Online Access:http://www.sciencedirect.com/science/article/pii/S2352340916300208
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spelling doaj-e5d6378dd48d4be1a0459287a809e8a72020-11-25T01:54:56ZengElsevierData in Brief2352-34092016-03-016965969Data for the identification of proteins and post-translational modifications of proteins associated to histones H3 and H4 in S. cerevisiae, using tandem affinity purification coupled with mass spectrometryM Luz Valero0Ramon Sendra1Mercè Pamblanco2Secció de Proteòmica, Servei Central de Suport a la Investigació Experimental (SCSIE), Universitat de València, C/Dr. Moliner 50, 46100 Burjassot, València, SpainDepartament de Bioquímica i Biologia Molecular, Universitat de València, C/ Dr. Moliner 50, 46100 Burjassot, Valencia, SpainDepartament de Bioquímica i Biologia Molecular, Universitat de València, C/ Dr. Moliner 50, 46100 Burjassot, Valencia, Spain; Corresponding author.Tandem affinity purification method (TAP) allows the efficient purification of native protein complexes which incorporate a target protein fused with the TAP tag. Purified multiprotein complexes can then be subjected to diverse types of proteomic analyses. Here we describe the data acquired after applying the TAP strategy on histones H3 and H4 coupled with mass spectrometry to identify associated proteins and protein post-translational modifications in the budding yeast, Saccharomyces cerevisiae. The mass spectrometry dataset described here consists of 14 files generated from four different analyses in a 5600 Triple TOF (Sciex) by information‐dependent acquisition (IDA) LC–MS/MS. The above files contain information about protein identification, protein relative abundance, and PTMs identification. The instrumental raw data from these files has been also uploaded to the ProteomeXchange Consortium via the PRIDE partner repository, with the dataset identifier PRIDE: http://www.ebi.ac.uk/pride/archive/projects/PXD002671 and http://dx.doi.org/10.6019/PXD002671. These data are discussed and interpreted in http://dx.doi.org/10.1016/j.jprot.2016.01.004. Valero et al. (2016) [1]. Keywords: Chromatin, Histones, Post-translational modifications, Proteomics, Tandem affinity purification, Yeasthttp://www.sciencedirect.com/science/article/pii/S2352340916300208
collection DOAJ
language English
format Article
sources DOAJ
author M Luz Valero
Ramon Sendra
Mercè Pamblanco
spellingShingle M Luz Valero
Ramon Sendra
Mercè Pamblanco
Data for the identification of proteins and post-translational modifications of proteins associated to histones H3 and H4 in S. cerevisiae, using tandem affinity purification coupled with mass spectrometry
Data in Brief
author_facet M Luz Valero
Ramon Sendra
Mercè Pamblanco
author_sort M Luz Valero
title Data for the identification of proteins and post-translational modifications of proteins associated to histones H3 and H4 in S. cerevisiae, using tandem affinity purification coupled with mass spectrometry
title_short Data for the identification of proteins and post-translational modifications of proteins associated to histones H3 and H4 in S. cerevisiae, using tandem affinity purification coupled with mass spectrometry
title_full Data for the identification of proteins and post-translational modifications of proteins associated to histones H3 and H4 in S. cerevisiae, using tandem affinity purification coupled with mass spectrometry
title_fullStr Data for the identification of proteins and post-translational modifications of proteins associated to histones H3 and H4 in S. cerevisiae, using tandem affinity purification coupled with mass spectrometry
title_full_unstemmed Data for the identification of proteins and post-translational modifications of proteins associated to histones H3 and H4 in S. cerevisiae, using tandem affinity purification coupled with mass spectrometry
title_sort data for the identification of proteins and post-translational modifications of proteins associated to histones h3 and h4 in s. cerevisiae, using tandem affinity purification coupled with mass spectrometry
publisher Elsevier
series Data in Brief
issn 2352-3409
publishDate 2016-03-01
description Tandem affinity purification method (TAP) allows the efficient purification of native protein complexes which incorporate a target protein fused with the TAP tag. Purified multiprotein complexes can then be subjected to diverse types of proteomic analyses. Here we describe the data acquired after applying the TAP strategy on histones H3 and H4 coupled with mass spectrometry to identify associated proteins and protein post-translational modifications in the budding yeast, Saccharomyces cerevisiae. The mass spectrometry dataset described here consists of 14 files generated from four different analyses in a 5600 Triple TOF (Sciex) by information‐dependent acquisition (IDA) LC–MS/MS. The above files contain information about protein identification, protein relative abundance, and PTMs identification. The instrumental raw data from these files has been also uploaded to the ProteomeXchange Consortium via the PRIDE partner repository, with the dataset identifier PRIDE: http://www.ebi.ac.uk/pride/archive/projects/PXD002671 and http://dx.doi.org/10.6019/PXD002671. These data are discussed and interpreted in http://dx.doi.org/10.1016/j.jprot.2016.01.004. Valero et al. (2016) [1]. Keywords: Chromatin, Histones, Post-translational modifications, Proteomics, Tandem affinity purification, Yeast
url http://www.sciencedirect.com/science/article/pii/S2352340916300208
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