Kinetic analysis of the effects of translation enhancers in translation initiation.

Shuntaro Takahashi; Hiroyuki Furusawa; Yoshihiro Shimizu; Takuya Ueda; Yoshio Okahata

Kinetic analysis of the effects of translation enhancers in translation initiation.

Shuntaro Takahashi, Hiroyuki Furusawa, Yoshihiro Shimizu, Takuya Ueda, Yoshio Okahata

Graduate School of Advanced Science and Engineering

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Abstract

Translation initiation is the most important step within a series of protein biosynthesis processes because the incorporation of ribosomes to a mRNA mainly determines efficiencies of translation. In bacteria, translation enhancers located on the 5' upstream of the Shine-Dargalno (SD) sequence on mRNAs are known to accelerate the efficiency of protein biosynthesis. To investigate the role of translation enhancers in translation initiation, we analyzed binding kinetics of a 30S ribosomal subunit to a mRNA immobilized on a 27 MHz quartz-crystal microbalance (QCM). The association constant (Ka) was rather low for the mRNA including a translation enhancer sequence compared with that for the mRNA without translation enhancers. These kinetic parameters suggest that translation enhancers destabilize the ribosome-mRNA complex on an SD sequence to move on the next step of decoding its mRNA.

Original language	English
Pages (from-to)	45-46
Number of pages	2
Journal	Nucleic acids symposium series (2004)
Issue number	51
Publication status	Published - 2007

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Takahashi, S., Furusawa, H., Shimizu, Y., Ueda, T., & Okahata, Y. (2007). Kinetic analysis of the effects of translation enhancers in translation initiation. Nucleic acids symposium series (2004), (51), 45-46.

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AU - Takahashi, Shuntaro

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AU - Okahata, Yoshio

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AB - Translation initiation is the most important step within a series of protein biosynthesis processes because the incorporation of ribosomes to a mRNA mainly determines efficiencies of translation. In bacteria, translation enhancers located on the 5' upstream of the Shine-Dargalno (SD) sequence on mRNAs are known to accelerate the efficiency of protein biosynthesis. To investigate the role of translation enhancers in translation initiation, we analyzed binding kinetics of a 30S ribosomal subunit to a mRNA immobilized on a 27 MHz quartz-crystal microbalance (QCM). The association constant (Ka) was rather low for the mRNA including a translation enhancer sequence compared with that for the mRNA without translation enhancers. These kinetic parameters suggest that translation enhancers destabilize the ribosome-mRNA complex on an SD sequence to move on the next step of decoding its mRNA.

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Kinetic analysis of the effects of translation enhancers in translation initiation.

Abstract

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