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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16
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pubmed:dateCreated |
1976-11-1
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pubmed:abstractText |
Phe-tRNAPhe species modified on the 3'-terminal ribose residue were investigated for their ability to participate in individual steps of the elongation cycle using eukaryotic ribosomes from reticulocytes. None of the Phe-tRNAs used, namely Phe-tRNAPhe-C-C-3'dA, Phe-tRNAPhe-C-C-3'-NH2A, and Phe-tRNAPhe-C-C-Aoxi-red, can function in the overall process. All modified Phe-tRNAPhe species can be bound nonenzymatically to ribosomes. Phe-tRNAPhe-C-C-3'NH2A exhibits exceptionally high binding at low Mg2+ concentration compared with Phe-tRNAPhe-C-C-A binding. Ac-Phe-tRNAPhe species prepared from the three modified tRNAs, when bound to the donor site, were devoid of donor activity. The enzymatic binding of both Phe-tRNAPhe-C-C-3'dA and Phe-tRNAPhe-C-C-3'NH2A is less efficient than that of Phe-tRNAPhe-C-C-A but these Phe-tRNAPhe species have acceptor activity. Phe-tRNAPhe-C-C--Aoxi-red is not a substrate for the EF-I promoted binding reaction and has no acceptor activity. The nonaminoacylated species, tRNAPhe-C-C-A, tRNAPhe-C-C-3'dA, and tRNAPhe-C-C-3'NH2A, bind to the ribosome to a larger extent than the corresponding aminoacylated tRNAs, both in the presence and in the absence of poly(U). Peptidyl-tRNAPhe-C-C-3'dA bound to the donor site cannot activate the acceptor site for EF-I promoted binding of Phe-tRNAPhe as does peptidyl-tRNAPhe-C-C-A. Further, it was observed that a correct codon-anticodon interaction influences the recognition of the 3' terminus of tRNA. Specificity of eukaryotic ribosomes for the 2'- and/or 3'-aminoacylated tRNA species is discussed and compared with the properties of Escherichia coli system.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine-tRNA Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/Poly U,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3639-46
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:782520-Binding Sites,
pubmed-meshheading:782520-Kinetics,
pubmed-meshheading:782520-Peptide Chain Elongation, Translational,
pubmed-meshheading:782520-Peptide Elongation Factors,
pubmed-meshheading:782520-Phenylalanine,
pubmed-meshheading:782520-Phenylalanine-tRNA Ligase,
pubmed-meshheading:782520-Poly U,
pubmed-meshheading:782520-RNA, Transfer,
pubmed-meshheading:782520-Ribosomes,
pubmed-meshheading:782520-Saccharomyces cerevisiae,
pubmed-meshheading:782520-Structure-Activity Relationship,
pubmed-meshheading:782520-Transcription, Genetic
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pubmed:year |
1976
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pubmed:articleTitle |
Properties of tRNA species modified in the 3'-terminal ribose moiety in an eukaryotic ribosomal system.
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pubmed:publicationType |
Journal Article
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