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rdf:type |
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lifeskim:mentions |
umls-concept:C0007625,
umls-concept:C0010715,
umls-concept:C0031453,
umls-concept:C0034493,
umls-concept:C0035286,
umls-concept:C0035711,
umls-concept:C0046571,
umls-concept:C0063775,
umls-concept:C0205349,
umls-concept:C0444930,
umls-concept:C0559956,
umls-concept:C0597295,
umls-concept:C0613220,
umls-concept:C0871161,
umls-concept:C1280500,
umls-concept:C1537998,
umls-concept:C1709915
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pubmed:issue |
7
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pubmed:dateCreated |
1977-11-30
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pubmed:abstractText |
Phe-tRNA Phe from yeast containing 2-thiocytidine or 5-iodocytidine in position 75 of the polynucleotide chain or Phe-tRNA Phe in which both positions 74 and 75 were substituted by 5-iodocytidine were investigated in the poly U-dependent polyphenylalanine synthesis on ribosomes from rabbit reticulocytes. Phe-tRNA Phe-Cps2CpA was nearly as active as the native Phe-tRNA Phe-CpCpA in the overall process. Phe-tRNA Phe-Cpi 5CpA as well as Phe-tRNA Phe-i5Cpi 5CpA were considerably less active than the native species. Investigation of individual steps of protein biosynthesis with these modified substrates revealed that the donor activity of peptidyl-tRNAs which contain 5-iodocytidine in their 3'-terminus is strongly imparied suggesting exacting structural requirements for the interaction of the CpCpA end of tRNA with the ribosomal P-site.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-1095417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-14172630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-4335860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-4339116,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-4571529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-4573492,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-4575980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-4580595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-4582194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-4593966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-4601427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-4612516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-4616173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-4854677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-4879821,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-5049048,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-5339543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-782520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/242797-967669
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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 |
Jul
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2205-12
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:242797-Animals,
pubmed-meshheading:242797-Base Sequence,
pubmed-meshheading:242797-Cytidine,
pubmed-meshheading:242797-Kinetics,
pubmed-meshheading:242797-Peptide Elongation Factors,
pubmed-meshheading:242797-Phenylalanine,
pubmed-meshheading:242797-Poly U,
pubmed-meshheading:242797-Protein Biosynthesis,
pubmed-meshheading:242797-RNA, Transfer, Amino Acyl,
pubmed-meshheading:242797-Rabbits,
pubmed-meshheading:242797-Reticulocytes,
pubmed-meshheading:242797-Ribosomes
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pubmed:year |
1977
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pubmed:articleTitle |
Properties of phenylalanine transfer ribonucleic acid with modified 3'-terminal end in protein biosynthesis using a rabbit reticulocyte cell-free system: effect of the replacement of cytidine residues from the CpCpA end of tRNA by 5-iodocytidine or 2-thiocytidine.
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pubmed:publicationType |
Journal Article
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