Modeling the reactive properties of tandemly activated tRNAs

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Tandemly activated tRNAs, bearing amino acid moieties at both the 2′ - and 3′-positions of the 3′-terminal adenosine moiety (A 76), have been shown to participate efficiently in protein synthesis [B. Wang, J. Zhou, M. Lodder, R. D. Anderson, III and S. M. Hecht, J. Biol. Chem., 2006, 281, 13865]. The mechanism by which such activated tRNAs are able to donate both amino acids to the growing polypeptide chain is not well understood. Here we report the chemical behavior and participation in protein synthesis of new bisaminoacyl derivatives of pdCpA and tRNA. Both amino moieties of the aminoacyl groups are shown to be important to enable participation in protein synthesis; paradoxically, they also confer an unanticipated chemical stability toward different nucleophiles. The results obtained suggest a model for participation of bisaminoacylated tRNAs in protein synthesis.

Original languageEnglish (US)
Pages (from-to)3292-3299
Number of pages8
JournalOrganic and Biomolecular Chemistry
Volume6
Issue number18
DOIs
StatePublished - 2008
Externally publishedYes

Fingerprint

protein synthesis
Transfer RNA
Amino Acid-Specific Transfer RNA
amino acids
Proteins
Bearings (structural)
Amino Acids
adenosines
Adenosine
Nucleophiles
nucleophiles
Chemical stability
polypeptides
Peptides
Derivatives

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Biochemistry

Cite this

Modeling the reactive properties of tandemly activated tRNAs. / Duca, Maria; Chen, Shengxi; Hecht, Sidney.

In: Organic and Biomolecular Chemistry, Vol. 6, No. 18, 2008, p. 3292-3299.

Research output: Contribution to journalArticle

@article{c8370282e46d4be49869408909a8be10,
title = "Modeling the reactive properties of tandemly activated tRNAs",
abstract = "Tandemly activated tRNAs, bearing amino acid moieties at both the 2′ - and 3′-positions of the 3′-terminal adenosine moiety (A 76), have been shown to participate efficiently in protein synthesis [B. Wang, J. Zhou, M. Lodder, R. D. Anderson, III and S. M. Hecht, J. Biol. Chem., 2006, 281, 13865]. The mechanism by which such activated tRNAs are able to donate both amino acids to the growing polypeptide chain is not well understood. Here we report the chemical behavior and participation in protein synthesis of new bisaminoacyl derivatives of pdCpA and tRNA. Both amino moieties of the aminoacyl groups are shown to be important to enable participation in protein synthesis; paradoxically, they also confer an unanticipated chemical stability toward different nucleophiles. The results obtained suggest a model for participation of bisaminoacylated tRNAs in protein synthesis.",
author = "Maria Duca and Shengxi Chen and Sidney Hecht",
year = "2008",
doi = "10.1039/b806790b",
language = "English (US)",
volume = "6",
pages = "3292--3299",
journal = "Organic and Biomolecular Chemistry",
issn = "1477-0520",
publisher = "Royal Society of Chemistry",
number = "18",

}

TY - JOUR

T1 - Modeling the reactive properties of tandemly activated tRNAs

AU - Duca, Maria

AU - Chen, Shengxi

AU - Hecht, Sidney

PY - 2008

Y1 - 2008

N2 - Tandemly activated tRNAs, bearing amino acid moieties at both the 2′ - and 3′-positions of the 3′-terminal adenosine moiety (A 76), have been shown to participate efficiently in protein synthesis [B. Wang, J. Zhou, M. Lodder, R. D. Anderson, III and S. M. Hecht, J. Biol. Chem., 2006, 281, 13865]. The mechanism by which such activated tRNAs are able to donate both amino acids to the growing polypeptide chain is not well understood. Here we report the chemical behavior and participation in protein synthesis of new bisaminoacyl derivatives of pdCpA and tRNA. Both amino moieties of the aminoacyl groups are shown to be important to enable participation in protein synthesis; paradoxically, they also confer an unanticipated chemical stability toward different nucleophiles. The results obtained suggest a model for participation of bisaminoacylated tRNAs in protein synthesis.

AB - Tandemly activated tRNAs, bearing amino acid moieties at both the 2′ - and 3′-positions of the 3′-terminal adenosine moiety (A 76), have been shown to participate efficiently in protein synthesis [B. Wang, J. Zhou, M. Lodder, R. D. Anderson, III and S. M. Hecht, J. Biol. Chem., 2006, 281, 13865]. The mechanism by which such activated tRNAs are able to donate both amino acids to the growing polypeptide chain is not well understood. Here we report the chemical behavior and participation in protein synthesis of new bisaminoacyl derivatives of pdCpA and tRNA. Both amino moieties of the aminoacyl groups are shown to be important to enable participation in protein synthesis; paradoxically, they also confer an unanticipated chemical stability toward different nucleophiles. The results obtained suggest a model for participation of bisaminoacylated tRNAs in protein synthesis.

UR - http://www.scopus.com/inward/record.url?scp=52649087854&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=52649087854&partnerID=8YFLogxK

U2 - 10.1039/b806790b

DO - 10.1039/b806790b

M3 - Article

C2 - 18802635

AN - SCOPUS:52649087854

VL - 6

SP - 3292

EP - 3299

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

SN - 1477-0520

IS - 18

ER -