The A-site finger in 23 S rRNA acts as a functional attenuator for translocation.

The A-site finger in 23 S rRNA acts as a functional attenuator for translocation. Research Abstract Details 

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The A-site finger in 23 S rRNA acts as a functional attenuator for translocation. Abstract Text:

Taeko Komoda,Neuza S Sato,Steven S Phelps,Naoki Namba,Simpson Joseph,Tsutomu Suzuki,

Helix 38 (H38) in 23 S rRNA, which is known as the "A-site finger (ASF)," is located in the intersubunit space of the ribosomal 50 S subunit and, together with protein S13 in the 30 S subunit, it forms bridge B1a. It is known that throughout the decoding process, ASF interacts directly with the A-site tRNA. Bridge B1a becomes disrupted by the ratchet-like rotation of the 30 S subunit relative to the 50 S subunit. This occurs in association with elongation factor G (EF-G)-catalyzed translocation. To further characterize the functional role(s) of ASF, variants of Escherichia coli ribosomes with a shortened ASF were constructed. The E. coli strain bearing such ASF-shortened ribosomes had a normal growth rate but enhanced +1 frameshift activity. ASF-shortened ribosomes showed normal subunit association but higher activity in poly(U)-dependent polyphenylalanine synthesis than the wild type (WT) ribosome at limited EF-G concentrations. In contrast, other ribosome variants with shortened bridge-forming helices 34 and 68 showed weak subunit association and less efficient translational activity than the WT ribosome. Thus, the higher translational activity of ASF-shortened ribosomes is caused by the disruption of bridge B1a and is not due to weakened subunit association. Single round translocation analyses clearly demonstrated that the ASF-shortened ribosomes have higher translocation activity than the WT ribosome. These observations indicate that the intrinsic translocation activity of ribosomes is greater than that usually observed in the WT ribosome and that ASF is a functional attenuator for translocation that serves to maintain the reading frame.

The A-site finger in 23 S rRNA acts as a functional attenuator for translocation. Publishing Authors By Initials

T Komoda,NS Sato,SS Phelps,N Namba,S Joseph,T Suzuki,

For similar enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: galactosidases: beta-galactosidase research abstracts see: enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: galactosidases: beta-galactosidase research

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The A-site finger in 23 S rRNA acts as a functional attenuator for translocation. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 281

Page Numbers: 32303-9

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 1

MONTH: 09

YEAR: 2006

The A-site finger in 23 S rRNA acts as a functional attenuator for translocation. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

The A-site finger in 23 S rRNA acts as a functional attenuator for translocation. Keywords Mesh Terms:

KEYWORDS: beta-Galactosidase

MESH TERMS: metabolism

Chemical & Substance for Abstract: The A-site finger in 23 S rRNA acts as a functional attenuator for translocation. Information

Substance Name: GTP Phosphohydrolases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for The A-site finger in 23 S rRNA acts as a functional attenuator for translocation.

AFFILIATION: Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.

Country: United States

AGENCY: United States NIGMS

GRANT: GM 65265

ACRONYM: GM

MEDLINETA: J Biol Chem

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