Jump to main content
Jump to site search

Issue 1, 2011
Previous Article Next Article

Synthesis of proteins with defined posttranslational modifications using the genetic noncanonical amino acid incorporation approach

Author affiliations

Abstract

Posttranslational modifications modulate the activities of most eukaryotic proteins and play a critical role in all aspects of cellular life. Understanding functional roles of these modifications requires homogenously modified proteins that are usually difficult to purify from their natural sources. An emerging powerful tool for synthesis of proteins with defined posttranslational modifications is to genetically encode modified amino acids in living cells and incorporate them directly into proteins during the protein translation process. Using this approach, homogenous proteins with tyrosine sulfation, tyrosine phosphorylation mimics, tyrosine nitration, lysine acetylation, lysine methylation, and ubiquitination have been synthesized in large quantities. In this review, we provide a brief introduction to protein posttranslational modifications and the genetic noncanonical amino acid (NAA) incorporation technique, then discuss successful applications of the genetic NAA incorporation approach to produce proteins with defined modifications, and end with challenges and ongoing methodology developments for synthesis of proteins with other modifications.

Graphical abstract: Synthesis of proteins with defined posttranslational modifications using the genetic noncanonical amino acid incorporation approach

Back to tab navigation

Article information


Submitted
30 Sep 2010
Accepted
21 Oct 2010
First published
19 Nov 2010

Mol. BioSyst., 2011,7, 38-47
Article type
Review Article

Synthesis of proteins with defined posttranslational modifications using the genetic noncanonical amino acid incorporation approach

W. R. Liu, Y. Wang and W. Wan, Mol. BioSyst., 2011, 7, 38
DOI: 10.1039/C0MB00216J

Search articles by author

Spotlight

Advertisements