A designed phenylalanyl-tRNA synthetase variant allows efficient in vivo incorporation of aryl ketone functionality into proteins

Deepshikha Datta; Pin Wang; Isaac S. Carrico; Stephen L. Mayo; David A. Tirrell

doi:10.1021/ja0177096

A designed phenylalanyl-tRNA synthetase variant allows efficient in vivo incorporation of aryl ketone functionality into proteins

Deepshikha Datta
, Pin Wang
, Isaac S. Carrico
, Stephen L. Mayo
, David A. Tirrell

Chemistry

Howard Hughes Medical Institute

Research output: Contribution to journal › Article › peer-review

131 Scopus citations

Abstract

Incorporation of non-natural amino acids into proteins in vivo expands the scope of protein synthesis and design. p-Acetylphenylalanine was incorporated into recombinant dihydrofolate reductase (DHFR) in Escherichia coli via a computationally designed mutant form of the phenylalanyl-tRNA synthetase of the host. DHFR outfitted with ketone functionality can be chemoselectively ligated with hydrazide reagents under mild conditions.

Original language	English
Pages (from-to)	5652-5653
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	124
Issue number	20
DOIs	https://doi.org/10.1021/ja0177096
State	Published - May 22 2002

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10.1021/ja0177096

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title = "A designed phenylalanyl-tRNA synthetase variant allows efficient in vivo incorporation of aryl ketone functionality into proteins",

abstract = "Incorporation of non-natural amino acids into proteins in vivo expands the scope of protein synthesis and design. p-Acetylphenylalanine was incorporated into recombinant dihydrofolate reductase (DHFR) in Escherichia coli via a computationally designed mutant form of the phenylalanyl-tRNA synthetase of the host. DHFR outfitted with ketone functionality can be chemoselectively ligated with hydrazide reagents under mild conditions.",

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AU - Datta, Deepshikha

AU - Wang, Pin

AU - Carrico, Isaac S.

AU - Mayo, Stephen L.

AU - Tirrell, David A.

PY - 2002/5/22

Y1 - 2002/5/22

N2 - Incorporation of non-natural amino acids into proteins in vivo expands the scope of protein synthesis and design. p-Acetylphenylalanine was incorporated into recombinant dihydrofolate reductase (DHFR) in Escherichia coli via a computationally designed mutant form of the phenylalanyl-tRNA synthetase of the host. DHFR outfitted with ketone functionality can be chemoselectively ligated with hydrazide reagents under mild conditions.

AB - Incorporation of non-natural amino acids into proteins in vivo expands the scope of protein synthesis and design. p-Acetylphenylalanine was incorporated into recombinant dihydrofolate reductase (DHFR) in Escherichia coli via a computationally designed mutant form of the phenylalanyl-tRNA synthetase of the host. DHFR outfitted with ketone functionality can be chemoselectively ligated with hydrazide reagents under mild conditions.

UR - https://www.scopus.com/pages/publications/0037157082

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DO - 10.1021/ja0177096

M3 - Article

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AN - SCOPUS:0037157082

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JO - Journal of the American Chemical Society

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ER -

A designed phenylalanyl-tRNA synthetase variant allows efficient in vivo incorporation of aryl ketone functionality into proteins

Abstract

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