2. Academic Validation
  3. Chemoproteomic Profiling of Cobalamin-Independent Methionine Synthases in Plants with a Covalent Probe

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

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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