Quality control of the elongation step of protein synthesis by tmRNP.

J. Wower, I. K. Wower, B. Kraal, Christian W Zwieb

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Trans-translation is a quality-control process, activated upon premature termination of protein elongation, which recycles stalled ribosomes and degrades incomplete polypeptides. These functions are facilitated by transfer-messenger RNA (tmRNA, also called 10Sa RNA or SsrA RNA), a small stable RNA molecule encoded by the SsrA gene found in bacteria, chloroplasts and mitochondria. Most tmRNAs consist of a tRNA- and an mRNA-like domain connected by up to four pseudoknots. Comparative sequence analysis provided the first insight into tmRNA secondary and three-dimensional structure. Studies of the E. coli tmRNA in vitro and in vivo demonstrated that tmRNA functions as a ribonucleoprotein (RNP) complex with elongation factor Tu (EF-Tu), protein SmpB and ribosomal protein S1. The tRNA-like and mRNA-like activities of tmRNA mark prematurely terminated proteins for degradation by attaching to their C-termini peptide tags, which are recognized by numerous proteases. Studies aimed at understanding the details of the molecular mechanisms of trans-translation are ongoing.

Original languageEnglish (US)
JournalJournal of Nutrition
Volume131
Issue number11
StatePublished - Nov 2001
Externally publishedYes

Fingerprint

Quality Control
quality control
protein synthesis
RNA
translation (genetics)
Transfer RNA
transfer RNA
ribonucleoproteins
Proteins
ribosomal proteins
messenger RNA
protein degradation
ribosomes
Messenger RNA
polypeptides
mitochondria
proteinases
sequence analysis
proteins
chloroplasts

ASJC Scopus subject areas

  • Medicine (miscellaneous)
  • Food Science

Cite this

Wower, J., Wower, I. K., Kraal, B., & Zwieb, C. W. (2001). Quality control of the elongation step of protein synthesis by tmRNP. Journal of Nutrition, 131(11).

Quality control of the elongation step of protein synthesis by tmRNP. / Wower, J.; Wower, I. K.; Kraal, B.; Zwieb, Christian W.

In: Journal of Nutrition, Vol. 131, No. 11, 11.2001.

Research output: Contribution to journalArticle

Wower, J, Wower, IK, Kraal, B & Zwieb, CW 2001, 'Quality control of the elongation step of protein synthesis by tmRNP.', Journal of Nutrition, vol. 131, no. 11.
Wower, J. ; Wower, I. K. ; Kraal, B. ; Zwieb, Christian W. / Quality control of the elongation step of protein synthesis by tmRNP. In: Journal of Nutrition. 2001 ; Vol. 131, No. 11.
@article{11c5a0c81e83446d915cf3caa84940af,
title = "Quality control of the elongation step of protein synthesis by tmRNP.",
abstract = "Trans-translation is a quality-control process, activated upon premature termination of protein elongation, which recycles stalled ribosomes and degrades incomplete polypeptides. These functions are facilitated by transfer-messenger RNA (tmRNA, also called 10Sa RNA or SsrA RNA), a small stable RNA molecule encoded by the SsrA gene found in bacteria, chloroplasts and mitochondria. Most tmRNAs consist of a tRNA- and an mRNA-like domain connected by up to four pseudoknots. Comparative sequence analysis provided the first insight into tmRNA secondary and three-dimensional structure. Studies of the E. coli tmRNA in vitro and in vivo demonstrated that tmRNA functions as a ribonucleoprotein (RNP) complex with elongation factor Tu (EF-Tu), protein SmpB and ribosomal protein S1. The tRNA-like and mRNA-like activities of tmRNA mark prematurely terminated proteins for degradation by attaching to their C-termini peptide tags, which are recognized by numerous proteases. Studies aimed at understanding the details of the molecular mechanisms of trans-translation are ongoing.",
author = "J. Wower and Wower, {I. K.} and B. Kraal and Zwieb, {Christian W}",
year = "2001",
month = "11",
language = "English (US)",
volume = "131",
journal = "Journal of Nutrition",
issn = "0022-3166",
publisher = "American Society for Nutrition",
number = "11",

}

TY - JOUR

T1 - Quality control of the elongation step of protein synthesis by tmRNP.

AU - Wower, J.

AU - Wower, I. K.

AU - Kraal, B.

AU - Zwieb, Christian W

PY - 2001/11

Y1 - 2001/11

N2 - Trans-translation is a quality-control process, activated upon premature termination of protein elongation, which recycles stalled ribosomes and degrades incomplete polypeptides. These functions are facilitated by transfer-messenger RNA (tmRNA, also called 10Sa RNA or SsrA RNA), a small stable RNA molecule encoded by the SsrA gene found in bacteria, chloroplasts and mitochondria. Most tmRNAs consist of a tRNA- and an mRNA-like domain connected by up to four pseudoknots. Comparative sequence analysis provided the first insight into tmRNA secondary and three-dimensional structure. Studies of the E. coli tmRNA in vitro and in vivo demonstrated that tmRNA functions as a ribonucleoprotein (RNP) complex with elongation factor Tu (EF-Tu), protein SmpB and ribosomal protein S1. The tRNA-like and mRNA-like activities of tmRNA mark prematurely terminated proteins for degradation by attaching to their C-termini peptide tags, which are recognized by numerous proteases. Studies aimed at understanding the details of the molecular mechanisms of trans-translation are ongoing.

AB - Trans-translation is a quality-control process, activated upon premature termination of protein elongation, which recycles stalled ribosomes and degrades incomplete polypeptides. These functions are facilitated by transfer-messenger RNA (tmRNA, also called 10Sa RNA or SsrA RNA), a small stable RNA molecule encoded by the SsrA gene found in bacteria, chloroplasts and mitochondria. Most tmRNAs consist of a tRNA- and an mRNA-like domain connected by up to four pseudoknots. Comparative sequence analysis provided the first insight into tmRNA secondary and three-dimensional structure. Studies of the E. coli tmRNA in vitro and in vivo demonstrated that tmRNA functions as a ribonucleoprotein (RNP) complex with elongation factor Tu (EF-Tu), protein SmpB and ribosomal protein S1. The tRNA-like and mRNA-like activities of tmRNA mark prematurely terminated proteins for degradation by attaching to their C-termini peptide tags, which are recognized by numerous proteases. Studies aimed at understanding the details of the molecular mechanisms of trans-translation are ongoing.

UR - http://www.scopus.com/inward/record.url?scp=0035513860&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035513860&partnerID=8YFLogxK

M3 - Article

C2 - 11694632

AN - SCOPUS:0035513860

VL - 131

JO - Journal of Nutrition

JF - Journal of Nutrition

SN - 0022-3166

IS - 11

ER -