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Genetic incorporation of histidine derivatives using an engineered pyrrolysyl-tRNA synthetase.
ACS Chem Biol. 2014 May 16; 9(5):1092-6.AC

Abstract

A polyspecific amber suppressor aminoacyl-tRNA synthetase/tRNA pair was evolved that genetically encodes a series of histidine analogues in both Escherichia coli and mammalian cells. In combination with tRNACUA(Pyl), a pyrrolysyl-tRNA synthetase mutant was able to site-specifically incorporate 3-methyl-histidine, 3-pyridyl-alanine, 2-furyl-alanine, and 3-(2-thienyl)-alanine into proteins in response to an amber codon. Substitution of His66 in the blue fluorescent protein (BFP) with these histidine analogues created mutant proteins with distinct spectral properties. This work further expands the structural and chemical diversity of unnatural amino acids (UAAs) that can be genetically encoded in prokaryotic and eukaryotic organisms and affords new probes of protein structure and function.

Authors+Show Affiliations

Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute , 10550 North Torrey Pines Road, La Jolla, California 92037, United States.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Letter
Research Support, N.I.H., Extramural

Language

eng

PubMed ID

24506189

Citation

Xiao, Han, et al. "Genetic Incorporation of Histidine Derivatives Using an Engineered pyrrolysyl-tRNA Synthetase." ACS Chemical Biology, vol. 9, no. 5, 2014, pp. 1092-6.
Xiao H, Peters FB, Yang PY, et al. Genetic incorporation of histidine derivatives using an engineered pyrrolysyl-tRNA synthetase. ACS Chem Biol. 2014;9(5):1092-6.
Xiao, H., Peters, F. B., Yang, P. Y., Reed, S., Chittuluru, J. R., & Schultz, P. G. (2014). Genetic incorporation of histidine derivatives using an engineered pyrrolysyl-tRNA synthetase. ACS Chemical Biology, 9(5), 1092-6. https://doi.org/10.1021/cb500032c
Xiao H, et al. Genetic Incorporation of Histidine Derivatives Using an Engineered pyrrolysyl-tRNA Synthetase. ACS Chem Biol. 2014 May 16;9(5):1092-6. PubMed PMID: 24506189.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Genetic incorporation of histidine derivatives using an engineered pyrrolysyl-tRNA synthetase. AU - Xiao,Han, AU - Peters,Francis B, AU - Yang,Peng-Yu, AU - Reed,Sean, AU - Chittuluru,Johnathan R, AU - Schultz,Peter G, Y1 - 2014/03/17/ PY - 2014/2/11/entrez PY - 2014/2/11/pubmed PY - 2015/1/6/medline SP - 1092 EP - 6 JF - ACS chemical biology JO - ACS Chem. Biol. VL - 9 IS - 5 N2 - A polyspecific amber suppressor aminoacyl-tRNA synthetase/tRNA pair was evolved that genetically encodes a series of histidine analogues in both Escherichia coli and mammalian cells. In combination with tRNACUA(Pyl), a pyrrolysyl-tRNA synthetase mutant was able to site-specifically incorporate 3-methyl-histidine, 3-pyridyl-alanine, 2-furyl-alanine, and 3-(2-thienyl)-alanine into proteins in response to an amber codon. Substitution of His66 in the blue fluorescent protein (BFP) with these histidine analogues created mutant proteins with distinct spectral properties. This work further expands the structural and chemical diversity of unnatural amino acids (UAAs) that can be genetically encoded in prokaryotic and eukaryotic organisms and affords new probes of protein structure and function. SN - 1554-8937 UR - https://www.unboundmedicine.com/medline/citation/24506189/Genetic_incorporation_of_histidine_derivatives_using_an_engineered_pyrrolysyl_tRNA_synthetase_ L2 - https://dx.doi.org/10.1021/cb500032c DB - PRIME DP - Unbound Medicine ER -