Chemoproteomic Profiling of Cobalamin-Independent Methionine Synthases in Plants with a Covalent Probe

  • J Agric Food Chem. 2020 Jul 29;68(30):8050-8056. doi: 10.1021/acs.jafc.0c03301.
Xin Chen  1  2 ,  Jingyuan Xu  1 ,  Nai-Kei Wong  3 ,  Suyun Zhong  1 ,  Mengquan Yang  2 ,  Zhen Liu  1 ,  Yan Lu  1 ,  Weichao Li  2 ,  Yiqing Zhou  1  2
Affiliations
  • 1. School of Biotechnology and Food Engineering, Changshu Institute of Technology, Changshu, Jiangsu 215500, China.
  • 2. CAS Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China.
  • 3. National Clinical Research Center for Infectious Diseases, Shenzhen Third People's Hospital, The Second Hospital Affiliated to Southern University of Science and Technology, Shenzhen 518112, China.
PMID: 32618189 DOI: 10.1021/acs.jafc.0c03301
Abstract

Cobalamin-independent methionine synthases (MS) are zinc-binding methyltransferases that catalyze de novo methionine biosynthesis in higher Plants, which are Enzymes critically involved in seed germination and plant growth. Here, we report a highly selective sulfonyl fluoride-based probe for chemoproteomic profiling of MS Enzymes in living systems of the model plant Arabidopsis thaliana, as implemented in in-gel-, mass spectrometry-, and imaging-based platforms. This probe holds promise for facilitating and accelerating fundamental research and industrial application of MS Enzymes, particularly in the contexts of MS1/2-targeting Herbicide screening and design.

Keywords
chemical probe; chemoproteomics; cobalamin-independent methionine synthases; covalent; herbicide.
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