Addition of a photocrosslinking amino acid to the genetic code of Escherichiacoli.

Abstract:

:Benzophenones are among the most useful photocrosslinking agents in biology. We have evolved an orthogonal aminoacyl-tRNA synthetase/tRNA pair that makes possible the in vivo incorporation of p-benzoyl-l-phenylalanine into proteins in Escherichia coli in response to the amber codon, TAG. This unnatural amino acid was incorporated with high translational efficiency and fidelity into the dimeric protein glutathione S-transferase. Irradiation resulted in efficient crosslinking (>50%) of the protein subunits. This methodology may prove useful for discovering and defining protein interactions in vitro and in vivo.

authors

Chin JW,Martin AB,King DS,Wang L,Schultz PG

doi

10.1073/pnas.172226299

keywords:

subject

Has Abstract

pub_date

2002-08-20 00:00:00

pages

11020-4

issue

17

eissn

0027-8424

issn

1091-6490

pii

172226299

journal_volume

99

pub_type

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