Chen Xiaohua group of Shanghai Institute of medicine, Chinese Academy of Sciences and Tang Zhuo group of Chengdu Institute of Biology

Recently, Chen Xiaohua group of Shanghai Institute of medicine, Chinese Academy of Sciences and Tang Zhuo group of Chengdu Institute of biology developed a new technology to capture protein interaction in living cells based on the development of new non natural amino acids This method has the advantages of time-space resolution and cross-linking site selectivity The research results were published in chem (DOI: 10.1016 / j.champr 2019.08.020) under the title of "genetically encoded residence selective photo crosslinker to capture protein protein interactions in living cells" Protein interaction plays a very important role in life activities Finding new protein interaction or function will help to clarify specific life processes and provide theoretical basis for the treatment of related diseases However, protein-protein interaction network is very complex, and it is very challenging to study protein-protein interaction in vivo Based on the gene codon expansion technology, the introduction of non natural amino acids with covalent cross-linking activity into the target proteins of living cells has become a powerful tool for studying protein-protein interaction in living cells The research team has developed a new method of spatiotemporal resolvable residue selective covalent crosslinking, aiming at the key problems such as complex structure of crosslinked peptide segments produced by the existing non selective protein crosslinking technology, difficult to analyze the mass spectrum data, false positive and so on It has successfully realized Effective capture of interacting protein complexes in living cells and subsequent mass spectrometry analysis Through the study of a variety of interacting proteins (such as acetylase and substrate), this technology can capture the weak protein interaction in living cells; the cross-linked peptide segment obtained from this technology can greatly simplify the analysis of mass spectrometry, as the direct evidence to determine protein interaction, determine the interface of interaction and verify the interaction between enzyme and specific substrate This method breaks through the bottleneck of traditional methods of protein interaction analysis and discovery to a certain extent, and is expected to be widely used in the study of weak, transient or dynamic protein interaction in living cells that are difficult to be found by traditional methods Chen Xiaohua, researcher of Shanghai Institute of medicine, Chinese Academy of Sciences, and Tang Zhuo, researcher of Chengdu Institute of biology are the co authors of this paper Hu Wei, Ph.D., of Chen Xiaohua's research group, is the first author of this paper Tan Minjia's research group of Institute of medicine participated in this work The research was supported by the mass spectrometry Technical Service Department of Shanghai Institute of medicine, and the project was supported by NSFC, Chinese Academy of Sciences and Shanghai Science and Technology Commission.