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The genesis of ribosome structure: how a protein generates RNA structure in real time.
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- Author(s): Woolstenhulme CJ;Woolstenhulme CJ; Hill WE
- Source:
Journal of molecular biology [J Mol Biol] 2009 Sep 25; Vol. 392 (3), pp. 645-56. Date of Electronic Publication: 2009 Jun 27.
- Publication Type:
Journal Article; Research Support, U.S. Gov't, Non-P.H.S.
- Language:
English
- Additional Information
- Source:
Publisher: Elsevier Country of Publication: Netherlands NLM ID: 2985088R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1089-8638 (Electronic) Linking ISSN: 00222836 NLM ISO Abbreviation: J Mol Biol Subsets: MEDLINE
- Publication Information:
Publication: Amsterdam : Elsevier
Original Publication: 1959- : London : Academic Press
- Subject Terms:
Nucleic Acid Conformation* ;
Protein Conformation* ;
RNA, Ribosomal, 16S*/
chemistry ;
RNA, Ribosomal, 16S*/
genetics ;
RNA, Ribosomal, 16S*/
metabolism;
Protein Subunits/
*chemistry ;
RNA/
*chemistry ;
Ribosomes/
*chemistry;
Amino Acid Sequence ;
Bacterial Proteins/
chemistry ;
Bacterial Proteins/
genetics ;
Bacterial Proteins/
metabolism ;
Base Sequence ;
Binding Sites ;
Crystallography, X-Ray ;
Molecular Sequence Data ;
Protein Binding ;
Protein Subunits/
genetics ;
Protein Subunits/
metabolism ;
RNA/
genetics ;
RNA, Bacterial/
chemistry ;
RNA, Bacterial/
genetics ;
RNA, Bacterial/
metabolism ;
Ribosomes/
genetics ;
Ribosomes/
metabolism ;
Sequence Alignment - Abstract:
Ribosomal subunit assembly is initiated by the binding of several primary binding proteins. Results from chemical modification studies show that 16S ribosomal RNA undergoes striking structural rearrangements when protein S17 is bound. For the first time, we are able to distinguish and order these structural rearrangements by using time-dependent chemical probing. Initially, protein S17 binds to a portion of helix 11, inducing a kink-turn in that helix that bends helix 7 toward the S17-helix 11 complex in a hairpin-like manner, allowing helix 7 to bind to protein S17. This structural change is rapidly stabilized by interactions at the distal and proximal ends of both RNA helices. Identifying the dynamic nature of interactions between RNA and proteins is not only essential in unraveling ribosome assembly, but also has more general application to all protein-RNA interactions.
- Accession Number:
0 (Bacterial Proteins)
0 (Protein Subunits)
0 (RNA, Bacterial)
0 (RNA, Ribosomal, 16S)
63231-63-0 (RNA)
- Publication Date:
Date Created: 20090701 Date Completed: 20091123 Latest Revision: 20090907
- Publication Date:
20221213
- Accession Number:
10.1016/j.jmb.2009.06.056
- Accession Number:
19563812
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