Proteomics data of SNF1-related protein kinase 2.4 interacting proteins revealed by immunoprecipitation-mass spectrometry

Tong Zhang; Jacqueline D Schneider; Chuwei Lin; Jin Koh; Sixue Chen

doi:10.1016/j.dib.2020.106326

Proteomics data of SNF1-related protein kinase 2.4 interacting proteins revealed by immunoprecipitation-mass spectrometry

Data Brief. 2020 Sep 20:32:106326. doi: 10.1016/j.dib.2020.106326. eCollection 2020 Oct.

Authors

Tong Zhang¹, Jacqueline D Schneider¹, Chuwei Lin¹, Jin Koh², Sixue Chen^{1

3

4

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Affiliations

¹ Department of Biology, University of Florida, Gainesville, FL 32610, USA.
² Interdisciplinary Center for Biotechnology Research, University of Florida, Gainesville, FL 32610, USA.
³ Genetics Institute, University of Florida, Gainesville, FL 32610, USA.
⁴ Plant Molecular and Cellular Biology Program, University of Florida, Gainesville, FL 32610, USA.

Abstract

Identification of kinase substrates is a prerequisite for elucidating the mechanism by which a kinase transduces internal or external stimuli to cellular responses. Conventional methods to profile this type of protein-protein interaction typically deal with one kinase-substrate pair at a time. Mass spectrometry-based proteomics, on the other hand, can determine putative kinase-substrate pairs at a large-scale in an unbiased manner. In this study, we identified the interacting partners of SNF1-related protein kinase 2.4 (SnRK2.4) via immunoprecipitation coupled with mass spectrometry. Proteins from stable transgenic Arabidopsis plants overexpressing a FLAG-tagged SnRK2.4 (cloned from Brassica napus) were pulled down using an anti-FLAG antibody. The protein components were then identified by mass spectrometry. In parallel, proteins from wild type plants were also analyzed, providing a list of nonspecific binding proteins that were further removed from the candidate SnRK2.4-interacting protein list. Our data identified over 30 putative SnRK2.4 interacting partners, which included many key players in stress responses, transport, and cellular metabolic processes.

Keywords: Immunoprecipitation-mass spectrometry; Protein-protein interaction; Proteomics; SNF1-related protein kinase 2.4.