Journal
DATA IN BRIEF
Volume 8, Issue -, Pages 56-60Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.dib.2016.05.014
Keywords
Protein-protein interactions; Arabidopsis thaliana; Plant biology; Circadian rhythms; Photoperiodism; Affinity purification; Mass spectrometry
Categories
Funding
- National Science Foundation [IOS-1456796, DBI-0922879]
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [1456796] Funding Source: National Science Foundation
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Tandem affinity purification coupled with mass spectrometry (TAP-MS) analysis is a powerful biochemical approach to identify protein-protein associations. Here we describe two datasets generated by a series of TAP-MS analyses to co-purify proteins associated with either ELF3 or ELF4 of the Evening Complex (EC) (Identification of Evening Complex Associated Proteins in Arabidopsis by Affinity Purification and Mass Spectrometry (Huang et al., 2016a) [1]) or proteins associated with PCH1, which is a newly identified output of the circadian clock to regulate photoperiodic growth in Arabidopsis thaliana (PCH1 integrates circadian and light-signaling pathways to control photoperiod-responsive growth in Arabidopsis (Huang et al. 2016b) [2]). We used either ELF3, ELF4 or PCH1 fused to a C-terminal tandem affinity tag (6xHis-3xFLAG) as baits and conducted purifications in various genetic mutant backgrounds. These data are discussed in recent publications [1'2], and are deposited at the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PRIDE: PXD002606 (for EC) and PRIDE: PXD003352 (for PCH1). (C) 2016 The Authors. Published by Elsevier Inc.
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