Rna-Protein Interactions in 30s Ribosomal Subunits Folding and Function of 16s Ribosomal Rna

Stern, S., Powers, T., Changchien, L. M., Noller, H. F. (May 1989) Rna-Protein Interactions in 30s Ribosomal Subunits Folding and Function of 16s Ribosomal Rna. Science (Washington D C), 244 (4906). pp. 783-790. ISSN :0036-8075

URL: http://www.ncbi.nlm.nih.gov/pubmed/2658053
DOI: 10.1126/science.2658053

Abstract

Chemical probing methods have been used to "footprint" 16S ribosomal RNA (rRNA) at each step during the in vitro assembly of twenty 30S subunit ribosomal proteins. These experiments yield information about the location of each protein relative to the structure of 16S rRNA and provide the basis for derivation of a detailed model for the three-dimensional folding of 16S rRNA. Several lines of evidence suggest that protein-dependent conformational changes in 16S rRNA play an important part in the cooperativity of ribosome assembly and in fine-tuning of the conformation and dynamics of 16S rRNA in the 30S subunit.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > analysis and processing > molecular interaction processing
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > gene expression
organs, tissues, organelles, cell types and functions > organelles, types and functions > ribosome
CSHL Authors:
Communities: CSHL labs
Depositing User: Gail Sherman
Date: 19 May 1989
Date Deposited: 23 Jun 2017 19:19
Last Modified: 23 Jun 2017 19:19
Related URLs:
URI: https://repository.cshl.edu/id/eprint/34909

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