Publication Date:
1978-12-01
Description:
Laser light scattering has been used to evaluate conformational differences between free 16S RNA and several specific protein-16S RNA complexes. Proteins that interact strongly with the 16S RNA early in subunit assembly stabilize the RNA chain against unfolding in 1 mM Mg2+ and actually promote the formation of a more compact teriary structure in 20 mM Mg2+. A vital function of these proteins may therfore consist in altering the configuration of the RNA so that further assembly reactions can take place.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bogdanov, A A -- Zimmermann, R A -- Wang, C C -- Ford, N C Jr -- New York, N.Y. -- Science. 1978 Dec 1;202(4371):999-1001.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/362531" target="_blank"〉PubMed〈/a〉
Keywords:
Bacterial Proteins
;
Diffusion
;
Escherichia coli
;
Nucleic Acid Conformation
;
Protein Binding
;
RNA, Bacterial
;
*RNA, Ribosomal
;
Ribonucleoproteins
;
*Ribosomal Proteins
;
Ribosomes/*ultrastructure
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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