Translation enhancer improves the ribosome liberation from translation initiation

Shuntaro Takahashi, Hiroyuki Furusawa, Takuya Ueda, Yoshio Okahata

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

For translation initiation in bacteria, the Shine-Dalgarno (SD) and anti-SD sequence of the 30S subunit play key roles for specific interactions between ribosomes and mRNAs to determine the exact position of the translation initiation region. However, ribosomes also must dissociate from the translation initiation region to slide toward the downstream sequence during mRNA translation. Translation enhancers upstream of the SD sequences of mRNAs, which likely contribute to a direct interaction with ribosome protein S1, enhance the yields of protein biosynthesis. Nevertheless, the mechanism of the effect of translation enhancers to initiate the translation is still unknown. In this paper, we investigated the effects of the SD and enhancer sequences on the binding kinetics of the 30S ribosomal subunits to mRNAs and their translation efficiencies. mRNAs with both the SD and translation enhancers promoted the amount of protein synthesis but destabilized the interaction between the 30S subunit and mRNA by increasing the dissociation rate constant (koff) of the 30S subunit. Based on a model for kinetic parameters, a 16-fold translation efficiency could be achieved by introducing a tandem repeat of adenine sequences (A20) between the SD and translation enhancer sequences. Considering the results of this study, translation enhancers with an SD sequence regulate ribosomal liberation from translation initiation to determine the translation efficiency of the downstream coding region.

Original languageEnglish
Pages (from-to)13096-13106
Number of pages11
JournalJournal of the American Chemical Society
Volume135
Issue number35
DOIs
Publication statusPublished - 2013 Sep 4
Externally publishedYes

Fingerprint

Ribosomes
Protein Biosynthesis
Messenger RNA
Proteins
Ribosome Subunits
Tandem Repeat Sequences
Adenine
Biosynthesis
Bacteria
Kinetic parameters
Rate constants
Kinetics

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Translation enhancer improves the ribosome liberation from translation initiation. / Takahashi, Shuntaro; Furusawa, Hiroyuki; Ueda, Takuya; Okahata, Yoshio.

In: Journal of the American Chemical Society, Vol. 135, No. 35, 04.09.2013, p. 13096-13106.

Research output: Contribution to journalArticle

Takahashi, Shuntaro ; Furusawa, Hiroyuki ; Ueda, Takuya ; Okahata, Yoshio. / Translation enhancer improves the ribosome liberation from translation initiation. In: Journal of the American Chemical Society. 2013 ; Vol. 135, No. 35. pp. 13096-13106.
@article{243c5658564e4994b029c8002b7ca9fe,
title = "Translation enhancer improves the ribosome liberation from translation initiation",
abstract = "For translation initiation in bacteria, the Shine-Dalgarno (SD) and anti-SD sequence of the 30S subunit play key roles for specific interactions between ribosomes and mRNAs to determine the exact position of the translation initiation region. However, ribosomes also must dissociate from the translation initiation region to slide toward the downstream sequence during mRNA translation. Translation enhancers upstream of the SD sequences of mRNAs, which likely contribute to a direct interaction with ribosome protein S1, enhance the yields of protein biosynthesis. Nevertheless, the mechanism of the effect of translation enhancers to initiate the translation is still unknown. In this paper, we investigated the effects of the SD and enhancer sequences on the binding kinetics of the 30S ribosomal subunits to mRNAs and their translation efficiencies. mRNAs with both the SD and translation enhancers promoted the amount of protein synthesis but destabilized the interaction between the 30S subunit and mRNA by increasing the dissociation rate constant (koff) of the 30S subunit. Based on a model for kinetic parameters, a 16-fold translation efficiency could be achieved by introducing a tandem repeat of adenine sequences (A20) between the SD and translation enhancer sequences. Considering the results of this study, translation enhancers with an SD sequence regulate ribosomal liberation from translation initiation to determine the translation efficiency of the downstream coding region.",
author = "Shuntaro Takahashi and Hiroyuki Furusawa and Takuya Ueda and Yoshio Okahata",
year = "2013",
month = "9",
day = "4",
doi = "10.1021/ja405967h",
language = "English",
volume = "135",
pages = "13096--13106",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "35",

}

TY - JOUR

T1 - Translation enhancer improves the ribosome liberation from translation initiation

AU - Takahashi, Shuntaro

AU - Furusawa, Hiroyuki

AU - Ueda, Takuya

AU - Okahata, Yoshio

PY - 2013/9/4

Y1 - 2013/9/4

N2 - For translation initiation in bacteria, the Shine-Dalgarno (SD) and anti-SD sequence of the 30S subunit play key roles for specific interactions between ribosomes and mRNAs to determine the exact position of the translation initiation region. However, ribosomes also must dissociate from the translation initiation region to slide toward the downstream sequence during mRNA translation. Translation enhancers upstream of the SD sequences of mRNAs, which likely contribute to a direct interaction with ribosome protein S1, enhance the yields of protein biosynthesis. Nevertheless, the mechanism of the effect of translation enhancers to initiate the translation is still unknown. In this paper, we investigated the effects of the SD and enhancer sequences on the binding kinetics of the 30S ribosomal subunits to mRNAs and their translation efficiencies. mRNAs with both the SD and translation enhancers promoted the amount of protein synthesis but destabilized the interaction between the 30S subunit and mRNA by increasing the dissociation rate constant (koff) of the 30S subunit. Based on a model for kinetic parameters, a 16-fold translation efficiency could be achieved by introducing a tandem repeat of adenine sequences (A20) between the SD and translation enhancer sequences. Considering the results of this study, translation enhancers with an SD sequence regulate ribosomal liberation from translation initiation to determine the translation efficiency of the downstream coding region.

AB - For translation initiation in bacteria, the Shine-Dalgarno (SD) and anti-SD sequence of the 30S subunit play key roles for specific interactions between ribosomes and mRNAs to determine the exact position of the translation initiation region. However, ribosomes also must dissociate from the translation initiation region to slide toward the downstream sequence during mRNA translation. Translation enhancers upstream of the SD sequences of mRNAs, which likely contribute to a direct interaction with ribosome protein S1, enhance the yields of protein biosynthesis. Nevertheless, the mechanism of the effect of translation enhancers to initiate the translation is still unknown. In this paper, we investigated the effects of the SD and enhancer sequences on the binding kinetics of the 30S ribosomal subunits to mRNAs and their translation efficiencies. mRNAs with both the SD and translation enhancers promoted the amount of protein synthesis but destabilized the interaction between the 30S subunit and mRNA by increasing the dissociation rate constant (koff) of the 30S subunit. Based on a model for kinetic parameters, a 16-fold translation efficiency could be achieved by introducing a tandem repeat of adenine sequences (A20) between the SD and translation enhancer sequences. Considering the results of this study, translation enhancers with an SD sequence regulate ribosomal liberation from translation initiation to determine the translation efficiency of the downstream coding region.

UR - http://www.scopus.com/inward/record.url?scp=84883672820&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84883672820&partnerID=8YFLogxK

U2 - 10.1021/ja405967h

DO - 10.1021/ja405967h

M3 - Article

VL - 135

SP - 13096

EP - 13106

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 35

ER -