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

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• 作者：M Luz Valero^a ; Ramon Sendra^b ; Mercè ; Pamblanco^b ; ^{merce.pamblanco@uv.es" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Chromatin ; Histones ; Post-translational modifications ; Proteomics ; Tandem affinity purification ; Yeast
• 刊名：Data in Brief
• 出版年：2016
• 出版时间：March 2016
• 年：2016
• 卷：6
• 期：Complete
• 页码：965-969
• 全文大小：187 K

文摘

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: PXD002671 and http://dx.doi.org.ezproxy.uned.es/10.6019/PXD002671. These data are discussed and interpreted in http://dx.doi.org.ezproxy.uned.es/10.1016/j.jprot.2016.01.004. Valero et al. (2016) [1].