Photo-lysine (Photo lysine)
(Synonyms: Photo lysine) 目录号 : GC30239光赖氨酸 (Photo lysine) 是一种新的基于赖氨酸的光反应性氨基酸,可捕获结合赖氨酸翻译后修饰的蛋白质。
Cas No.:1863117-91-2
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Photo-lysine, a new lysine-based photo-reactive amino acid, captures proteins that bind lysine post-translational modifications.
Photo-lysine is designed and synthesized by incorporating a photo-cross-linker (diazirine) into the side chain of natural lysine. Photo-lysine, which is readily incorporated into proteins by native mammalian translation machinery, can be used to capture and identify proteins that recognize lysine post-translational modifications (PTMs), including 'readers' and 'erasers' of histone modifications. Photo-lysine can be incorporated into MDH2 and mediate photo-cross-linking to fix protein-protein interactions in cells. UV irradiation of cells in the presence of photo-lysine induced robust cross-linking of HSP90β and HSP60. Photo-lysine has higher efficiency than photo-leucine for photo-cross-linking of the two chaperone proteins. Photo-lysine enables capture of the heterodimer of proteins Ku70 and Ku80 within a protein complex. Photo-lysine enables identification of histone- and chromatin-binding proteins[1].
[1]. Yang T, et al. Photo-lysine captures proteins that bind lysine post-translational modifications. Nat Chem Biol. 2016 Feb;12(2):70-2.
Cas No. | 1863117-91-2 | SDF | |
别名 | Photo lysine | ||
Canonical SMILES | NCCC1(N=N1)C[C@@H](C(O)=O)N | ||
分子式 | C6H12N4O2 | 分子量 | 172.19 |
溶解度 | Soluble in Water | 储存条件 | Store at -20°C |
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5 mM | 1.1615 mL | 5.8075 mL | 11.6151 mL |
10 mM | 0.5808 mL | 2.9038 mL | 5.8075 mL |
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Photo-lysine captures proteins that bind lysine post-translational modifications
Post-translational modifications (PTMs) have key roles in regulating protein-protein interactions in living cells. However, it remains a challenge to identify these PTM-mediated interactions. Here we develop a new lysine-based photo-reactive amino acid, termed photo-lysine. We demonstrate that photo-lysine, which is readily incorporated into proteins by native mammalian translation machinery, can be used to capture and identify proteins that recognize lysine PTMs, including 'readers' and 'erasers' of histone modifications.
Genetically Encoded Photoaffinity Histone Marks
Posttranslational modifications (PTMs) of lysine are crucial histone marks that regulate diverse biological processes. The functional roles and regulation mechanism of many newly identified lysine PTMs, however, remain yet to be understood. Here we report a photoaffinity crotonyl lysine (Kcr) analogue that can be genetically and site-specifically incorporated into histone proteins. This, in conjunction with the genetically encoded photo-lysine as a "control probe", enables the capture and identification of enzymatic machinery and/or effector proteins for histone lysine crotonylation.
Comparative analysis of polyspecificity of the endogenous tRNA synthetase of different expression host towards photocrosslinking amino acids using an in silico approach
Photo-induced covalent crosslinking has emerged as the powerful strategy for analyzing and characterizing the protein-protein interaction and mapping protein 3D conformations. In the last decades, a number of photocrosslinking amino acids have been reported but only a few have been efficiently utilized for photocrosslinking purposes. Recently, incorporation of diazirine containing photoactivatable analogs such as photo-methionine, photo-leucine, photo-isoleucine and photo-lysine into target proteins were accomplished in live cells (Human A549cells, HEK 293) by depleting corresponding natural amino acid and supplementing these analogs in the medium. Likewise, incorporation of photo-methionine and photo-leucine is also reported in E. coli. Incorporation of these unnatural amino acids were demonstrated only in a limited number species, thereby conventional methods have been utilized for the protein-protein interaction study in other species. With this in mind, we studied in silico analysis of polyspecificity of four endogenous tRNA synthetases (LeuRS, IleRS, MetRS, and LysRS) from six different species such as Escherichia coli, Pseudomonas fluorescens, Corynebacterium glutamicum, Saccharomyces cerevisiae, Aspergillus oryzae and Homo sapiens towards its photocrosslinking amino acids. In addition, here we describe the active site similarity of different protein bio-factories. Based on the active site similarity and similar binding mode, we predicted that the endogenous tRNA synthetases of all the species are reactive to corresponding photoactivatable analogs. This is the first in silico study to demonstrate that the photocrosslinking unnatural amino acids are recognized by the endogenous tRNA synthetases of different protein expression biofactories.