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

Mahdavi, A., Hamblin, G. D., Jindal, G. A., Bagert, J. D., Dong, C., Sweredoski, M. J., et al. (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.

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 Creators:
Mahdavi, Alborz, Author
Hamblin, Graham D., Author
Jindal, Granton A., Author
Bagert, John D., Author
Dong, Cathy, Author
Sweredoski, Michael J., Author
Hess, Sonja, Author
Schuman, Erin M.1, Author           
Tirrell, David A., Author
Affiliations:
1Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society, ou_2461710              

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Free keywords: Genetics,Labeling,Peptides and proteins,Protein dynamics,Protein identification
 Abstract: 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.

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Language(s): eng - English
 Dates: 2015-08-242016-03-18
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 723887
DOI: 10.1021/jacs.5b08980
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Title: Journal of the American Chemical Society
  Alternative Title : JACS
Source Genre: Journal
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Pages: - Volume / Issue: 138 Sequence Number: - Start / End Page: 4278 - 4281 Identifier: -