tRNA Analogues Research Articles

Photoaffinity reagents for modification of aminoacyl-tRNA synthetases

Up to now, a few derivatives of aminoacyl-tRNA with a reactive group attached to the aminoacyl residue [l-4] and a reactive analog of an amino acid [4] have been used for the affinity labeling of aminoacyltRNA synthetases (EC 6.1 .l). For detailed investigation of the active centers of these enzymes, it is necessary to prepare tRNA analogs bearing reactive group at some other sites of the tRNA molecule, as well as reactive ATP analogs. The present communication describes ATP and tRNA analogs containing a photoreactive azido group, namely ATP-y-p-azidoanilide and tRNA containing the Ns Cg Ha NH-CO-CH2 -group at iached to a 4thiouridine residue. The possibility of using the photoreactivity of the 4-thiouridine residue of tRNA for photoaffinity labeling of phe-RSase* is also reported; a similar approach has been proposed by other workers [6] who described a light induced reaction of 4-thiouridine triphosphate with RNA polymerase.

Affinity labeling of Escherichia coli ribosomal proteins with an analog of the natural initiator tRNA.

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAffinity labeling of Escherichia coli ribosomal proteins with an analog of the natural initiator tRNAMohan Sopori, Maria Pellegrini, Peter Lengyel, and Charles R. CantorCite this: Biochemistry 1974, 13, 26, 5432–5439Publication Date (Print):December 1, 1974Publication History Published online1 May 2002Published inissue 1 December 1974https://doi.org/10.1021/bi00723a030RIGHTS & PERMISSIONSArticle Views18Altmetric-Citations26LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (949 KB) Get e-Alerts Get e-Alerts

A new simpler photoaffinity analogue of peptidyl tRNA.

The synthesis of the n-hydroxysuccinimide ester of N-(2-nitro-4-azidophenyl)glycine (NAG) is described. This reacts with E. coli phe-tRNA(Phe) to yield the photoaffinity label NAG-Phe-tRNA(Phe). This peptidyl tRNA analogue binds correctly to the peptidyl site of the E. coli ribosome. The only significant covalent products found after irradiation of a peptidyl site bound NAG-Phe-tRNA(Phe)-70S-poly(U) complex are 50S proteins L11 and L18. After irradiation the complex can still bind [(3)H]Phe-tRNA to the amino acyl site and participate in peptide bond formation with the covalently attached NAG-Phe moiety. Alternatively, one can allow peptide bond formation to occur first, prior to photolysis. The reaction products are still L11 and L18. Hence, both of these two proteins appear to be centrally located at the peptidyl transferase center.