Acetylation modification has the potential to regulate the vitality of aarRS amino.

On April 28, the international academic journal Journal of Biochemistry published online the latest findings of the Wang Endo Research Group of the Center for Excellence in Molecular Cell Science/Biochemistry and Cell Biology, Shanghai Institute of Life Sciences, Chinese Academy of Sciences: Acetylation of lysine-amino groups regulators aminoacyl-tRNA synthetase activityy in Escherichia coli.
aminoacyl-tRNA synthase (aminoacyl-tRNA synthetase, aaRS) catalyses the esterification reaction between aminoline acids and the corresponding tRNA substrates to produce aminoacyl-tRNA (aminoacyl-tRNA), which provides the raw material for protein synthesis on nuclear glycogens.
the similarity of the position of the catalytic domain and aminoated reaction on the tRNA end rna, aaRS can be divided into classes I and II.
-tRNA synthase (leucyl-tRNA synthetase, LeuRS), arginyl-tRNA synthase (arginyl-tRNA sythetase, ArgRS) belongs to Class I enzymes.
There have been reports that some aarRS phosphorylation modifications may be involved in signaling path paths such as E. coli resistance mechanisms or oxidative stress in mammalian cells, but there has been little in-depth research on other types of post-translation modifications on aaaRS, such as acetylation modifications.
proteomics analysis showed that aaaRS from E. coli to humans (Homo sapiens) had acetylation modifications, and some of the lysine residues identified as having acetylation modifications were conservative.
under wang Endo's guidance, Ph.D. student Ye Qing et al. studied the effects of acetylation modification of aaaRS in E. coli on enzyme vitality.
they obtained bit information on LeuRS and AargRS acetylation modifications in E. coli through mass spectrometry, and three bits on EcLeuRS (Lys619, Lys6) were discovered using glutamine (Glutamine, Glu) scans (Glu scanning, simulating Lys with acetylation modifications) 24 and Lys809) and 2 bits on EcArgRS (Lys126 and Lys408) play an important role in the catalytic vitality of enzymes;
After analyzing the properties of the enzymes modified with acetylation above, they found that the acetylation modified enzymes of the above Lys residues reduced the active vitality of amino acids and the affinity between enzymes and their corresponding tRNAs, reducing or losing the aminoization vitality of enzymes.
addition, they found through in-body experiments that a high-energy compound acetylphosphate (acetyl-phosphate, AcP) and silent information regulator 2-related enzymes (silent information regulator 2-enzymes, Sirtuin) family of deacetylase CobB may be involved in acetylation and deacetylation ecles.
above results reveal the potential regulatory function of acetylation modification to aarRS aminoamide vitality, and for the first time it is suggested that acetylation modification may control the vitality of aaaRS as a translation level switch, thus affecting the protein translation process.
the study was funded by the Ministry of Science and Technology, the National Natural Science Foundation of China and the Chinese Academy of Sciences.
data collection is supported by the Public Technical Service Center of the Institute of Biotechnology and Cells.
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