N-Acetyl lysyl-tRNA synthetases evolved by a CcdB-based selection possess N-acetyl lysine specificity in vitro and in vivo

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Posttranslational modifications play a crucial role in modulating protein structure and function. Genetic incorporation of unnatural amino acids into a specific site of a protein facilitates the systematic study of protein modifications including acetylation. We here report the directed evolution of pyrrolysyl-tRNA synthetase (PylRS) from Methanosarcina mazei to create N-acetyl lysyl-tRNA synthetases (AcKRSs) using a new selection system based on the killing activity of the toxic ccdB gene product. The amino acid specificity of these and of published [1,2] AckRSs was tested in vitro and in vivo, and the enzyme-kinetic properties of the AckRSs were evaluated for the first time. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publisher
ELSEVIER SCIENCE BV
Issue Date
2012-03
Language
English
Article Type
Article
Keywords

ESCHERICHIA-COLI; GENETIC-CODE; PROTEIN; PYRROLYSINE; MUTANTS; DESIGN

Citation

FEBS LETTERS, v.586, no.6, pp.729 - 733

ISSN
0014-5793
DOI
10.1016/j.febslet.2012.01.029
URI
http://hdl.handle.net/10203/103140
Appears in Collection
CH-Journal Papers(저널논문)
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