Chemoproteomic Profiling of Cobalamin-Independent Methionine Synthases in Plants with a Covalent Probe.
Xin ChenJingyuan XuNai-Kei WongSuyun ZhongMengquan YangZhen LiuYan LuWeichao LiYiqing ZhouPublished in: Journal of agricultural and food chemistry (2020)
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.
Keyphrases
- mass spectrometry
- plant growth
- arabidopsis thaliana
- multiple sclerosis
- ms ms
- liquid chromatography
- high resolution
- living cells
- quantum dots
- capillary electrophoresis
- gas chromatography
- high performance liquid chromatography
- amino acid
- heavy metals
- wastewater treatment
- risk assessment
- photodynamic therapy
- artificial intelligence
- transcription factor
- big data
- wound healing
- deep learning
- tandem mass spectrometry
- drug delivery
- single molecule
- fluorescence imaging
- binding protein