Tandemly activated tRNAs as participants in protein synthesis

Bixun Wang, Jia Zhou, Michiel Lodder, Raymond D. Anderson, Sidney M. Hecht

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

While all studies of protein synthesis to date have employed monoaminoacylated transfer RNAs, there have been reports that bisphenylalanyl-tRNA is formed by Thermus thermophilus phenylalanyl-tRNA synthetase. Such tandemly activated tRNAs have now been prepared by chemicoenzymatic techniques and are shown to function in both prokaryotic and mammalian protein synthesizing systems. They exhibit characteristics consistent with their possible utility under extreme conditions in natural systems and have important potential advantages for protein elaboration in cell free systems. Mechanistically, the bisaminoacylated tRNAs bind to the ribosomal A-site and utilize the aminoacyl moiety attached to the 3′-position of the terminal adenosine for addition to the growing polypeptide chain. Following translocation to the P-site and transfer of the formed peptidyl moiety, the donor tRNA dissociates from the ribosome as a monoaminoacylated tRNA capable of functioning in a subsequent polypeptide elongation step.

Original languageEnglish (US)
Pages (from-to)13865-13868
Number of pages4
JournalJournal of Biological Chemistry
Volume281
Issue number20
DOIs
StatePublished - May 19 2006
Externally publishedYes

Fingerprint

Transfer RNA
Proteins
Phenylalanine-tRNA Ligase
Thermus thermophilus
Peptides
Cell-Free System
Ribosomes
Adenosine
Elongation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Tandemly activated tRNAs as participants in protein synthesis. / Wang, Bixun; Zhou, Jia; Lodder, Michiel; Anderson, Raymond D.; Hecht, Sidney M.

In: Journal of Biological Chemistry, Vol. 281, No. 20, 19.05.2006, p. 13865-13868.

Research output: Contribution to journalArticle

Wang, Bixun ; Zhou, Jia ; Lodder, Michiel ; Anderson, Raymond D. ; Hecht, Sidney M. / Tandemly activated tRNAs as participants in protein synthesis. In: Journal of Biological Chemistry. 2006 ; Vol. 281, No. 20. pp. 13865-13868.
@article{9b39af16c0e549f5bb1104aa3ee3f999,
title = "Tandemly activated tRNAs as participants in protein synthesis",
abstract = "While all studies of protein synthesis to date have employed monoaminoacylated transfer RNAs, there have been reports that bisphenylalanyl-tRNA is formed by Thermus thermophilus phenylalanyl-tRNA synthetase. Such tandemly activated tRNAs have now been prepared by chemicoenzymatic techniques and are shown to function in both prokaryotic and mammalian protein synthesizing systems. They exhibit characteristics consistent with their possible utility under extreme conditions in natural systems and have important potential advantages for protein elaboration in cell free systems. Mechanistically, the bisaminoacylated tRNAs bind to the ribosomal A-site and utilize the aminoacyl moiety attached to the 3′-position of the terminal adenosine for addition to the growing polypeptide chain. Following translocation to the P-site and transfer of the formed peptidyl moiety, the donor tRNA dissociates from the ribosome as a monoaminoacylated tRNA capable of functioning in a subsequent polypeptide elongation step.",
author = "Bixun Wang and Jia Zhou and Michiel Lodder and Anderson, {Raymond D.} and Hecht, {Sidney M.}",
year = "2006",
month = "5",
day = "19",
doi = "10.1074/jbc.C600018200",
language = "English (US)",
volume = "281",
pages = "13865--13868",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "20",

}

TY - JOUR

T1 - Tandemly activated tRNAs as participants in protein synthesis

AU - Wang, Bixun

AU - Zhou, Jia

AU - Lodder, Michiel

AU - Anderson, Raymond D.

AU - Hecht, Sidney M.

PY - 2006/5/19

Y1 - 2006/5/19

N2 - While all studies of protein synthesis to date have employed monoaminoacylated transfer RNAs, there have been reports that bisphenylalanyl-tRNA is formed by Thermus thermophilus phenylalanyl-tRNA synthetase. Such tandemly activated tRNAs have now been prepared by chemicoenzymatic techniques and are shown to function in both prokaryotic and mammalian protein synthesizing systems. They exhibit characteristics consistent with their possible utility under extreme conditions in natural systems and have important potential advantages for protein elaboration in cell free systems. Mechanistically, the bisaminoacylated tRNAs bind to the ribosomal A-site and utilize the aminoacyl moiety attached to the 3′-position of the terminal adenosine for addition to the growing polypeptide chain. Following translocation to the P-site and transfer of the formed peptidyl moiety, the donor tRNA dissociates from the ribosome as a monoaminoacylated tRNA capable of functioning in a subsequent polypeptide elongation step.

AB - While all studies of protein synthesis to date have employed monoaminoacylated transfer RNAs, there have been reports that bisphenylalanyl-tRNA is formed by Thermus thermophilus phenylalanyl-tRNA synthetase. Such tandemly activated tRNAs have now been prepared by chemicoenzymatic techniques and are shown to function in both prokaryotic and mammalian protein synthesizing systems. They exhibit characteristics consistent with their possible utility under extreme conditions in natural systems and have important potential advantages for protein elaboration in cell free systems. Mechanistically, the bisaminoacylated tRNAs bind to the ribosomal A-site and utilize the aminoacyl moiety attached to the 3′-position of the terminal adenosine for addition to the growing polypeptide chain. Following translocation to the P-site and transfer of the formed peptidyl moiety, the donor tRNA dissociates from the ribosome as a monoaminoacylated tRNA capable of functioning in a subsequent polypeptide elongation step.

UR - http://www.scopus.com/inward/record.url?scp=33744939245&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33744939245&partnerID=8YFLogxK

U2 - 10.1074/jbc.C600018200

DO - 10.1074/jbc.C600018200

M3 - Article

VL - 281

SP - 13865

EP - 13868

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 20

ER -