日本語
 
Help Privacy Policy ポリシー/免責事項
  詳細検索ブラウズ

アイテム詳細


公開

学術論文

Engineered Aminoacyl-tRNA Synthetase for Cell-Selective Analysis of Mammalian Protein Synthesis

MPS-Authors
/persons/resource/persons208206

Schuman,  Erin M.
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

External Resource

https://pubmed.ncbi.nlm.nih.gov/26991063/
(全文テキスト(全般))

Fulltext (restricted access)
There are currently no full texts shared for your IP range.
フルテキスト (公開)
公開されているフルテキストはありません
付随資料 (公開)
There is no public supplementary material available
引用

Mahdavi, A., Hamblin, G. D., Jindal, G. A., Bagert, J. D., Dong, C., Sweredoski, M. J., Hess, S., Schuman, E. M., & Tirrell, D. A. (2016). Engineered Aminoacyl-tRNA Synthetase for Cell-Selective Analysis of Mammalian Protein Synthesis. Journal of the American Chemical Society, 138, 4278-4281. doi:10.1021/jacs.5b08980.


引用: https://hdl.handle.net/11858/00-001M-0000-002E-58D5-6
要旨
Methods for cell-selective analysis of proteome dynamics will facilitate studies of biological processes in multicellular organisms. Here we describe a mutant murine methionyl-tRNA synthetase (designated L274GMmMetRS) that charges the noncanonical amino acid azidonorleucine (Anl) to elongator tRNA(Met) in hamster (CHO), monkey (COS7), and human (HeLa) cell lines. Proteins made in cells that express the synthetase can be labeled with Anl, tagged with dyes or affinity reagents, and enriched on affinity resin to facilitate identification by mass spectrometry. The method does not require expression of orthogonal tRNAs or depletion of canonical amino acids. Successful labeling of proteins with Anl in several mammalian cell lines demonstrates the utility of L274GMmMetRS as a tool for cell-selective analysis of mammalian protein synthesis.