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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1991-7-17
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pubmed:abstractText |
The E. coli 16 S rRNA with single-site breaks centered at position 777 or 785 was obtained by RNase H site-specific cleavage of rRNA. Spontaneous dissociation of the cleaved 16 S rRNA into fragments occurred under 'native' conditions. The reassociation of the 16 S rRNA fragments was possible only in the presence of ribosomal proteins. The combination of S4 and S16(S17) ribosomal proteins interacting mainly with the 5'-end domain of 16 S rRNA was sufficient for reassociation of the fragments. The 30 S subunits with fragmented RNA at ca. 777 region retained some poly(U)-directed protein synthetic activity.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
283
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
251-4
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1646122-Base Composition,
pubmed-meshheading:1646122-Base Sequence,
pubmed-meshheading:1646122-Centrifugation, Density Gradient,
pubmed-meshheading:1646122-Endoribonucleases,
pubmed-meshheading:1646122-Escherichia coli,
pubmed-meshheading:1646122-Kinetics,
pubmed-meshheading:1646122-Molecular Sequence Data,
pubmed-meshheading:1646122-Peptide Biosynthesis,
pubmed-meshheading:1646122-Peptides,
pubmed-meshheading:1646122-Poly U,
pubmed-meshheading:1646122-Protein Biosynthesis,
pubmed-meshheading:1646122-RNA, Ribosomal, 16S,
pubmed-meshheading:1646122-Ribonuclease H,
pubmed-meshheading:1646122-Ribonucleoproteins,
pubmed-meshheading:1646122-Ribosomal Proteins,
pubmed-meshheading:1646122-Ribosomes
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pubmed:year |
1991
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pubmed:articleTitle |
RNA-RNA and RNA-protein interactions in 30 S ribosomal subunits. Association of 16 S rRNA fragments in the presence of ribosomal proteins.
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pubmed:affiliation |
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University USSR.
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pubmed:publicationType |
Journal Article
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