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rdf:type |
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|
lifeskim:mentions |
|
|
pubmed:issue |
2
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pubmed:dateCreated |
1976-2-2
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|
pubmed:abstractText |
50-S subunits were washed with LiCl solutions of different concentrations. After washing with 1 M LiCl solution the particles lost their ability to attach either to 30-S subunits or to the AUG - 30-S subunit - fMet-tRNAfMet complex or to a poly(U) - 30-S subunit - Phe-tRNAPhe complex. Those proteins which were removed by LiCl were fractionated on a Sephadex G-100 column. Of the fractionated proteins only the combinations L1 and L11 or L1 and L16 were essential for the association of 50-S 1.0 cores (particles prepared by washing 50-S subunits in 1.0 M LiCl) with 30-S subunits. These three proteins were also required for the formation of a stable complex between 50-S 1.0 cores, mRNA, 30-S subunits and aminoacyl-tRNA.
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pubmed:language |
eng
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pubmed:journal |
|
|
pubmed:citationSubset |
IM
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|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
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|
pubmed:month |
Oct
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|
pubmed:issn |
0014-2956
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|
pubmed:author |
|
|
pubmed:issnType |
Print
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|
pubmed:day |
15
|
|
pubmed:volume |
58
|
|
pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
501-10
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|
pubmed:dateRevised |
2007-7-23
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|
pubmed:meshHeading |
pubmed-meshheading:1102306-Binding Sites,
pubmed-meshheading:1102306-Chlorides,
pubmed-meshheading:1102306-Chromatography, Gel,
pubmed-meshheading:1102306-Escherichia coli,
pubmed-meshheading:1102306-Lithium,
pubmed-meshheading:1102306-Methionine,
pubmed-meshheading:1102306-Molecular Weight,
pubmed-meshheading:1102306-Peptide Chain Initiation, Translational,
pubmed-meshheading:1102306-Phenylalanine,
pubmed-meshheading:1102306-Poly U,
pubmed-meshheading:1102306-Puromycin,
pubmed-meshheading:1102306-RNA, Transfer,
pubmed-meshheading:1102306-Ribosomal Proteins,
pubmed-meshheading:1102306-Ribosomes,
pubmed-meshheading:1102306-Transfer RNA Aminoacylation
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|
pubmed:year |
1975
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|
pubmed:articleTitle |
The importance of Escherichia coli ribosomal proteins L1, L11 and L16 for the association of ribosomal subunits and the formation of the 70-S initiation complex.
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pubmed:publicationType |
Journal Article
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