anticodon and 2-thiocytidine

anticodon has been researched along with 2-thiocytidine* in 2 studies

Other Studies

2 other study(ies) available for anticodon and 2-thiocytidine

Article	Year
The decoding region of 16S RNA; a cross-linking study of the ribosomal A, P and E sites using tRNA derivatized at position 32 in the anticodon loop. The EMBO journal, 1994, Jun-01, Volume: 13, Issue:11 A photo-reactive diazirine derivative was attached to the 2-thiocytidine residue at position 32 of tRNA(Arg)I from Escherichia coli. This modified tRNA was bound under suitable conditions to the A, P or E site of E.coli ribosomes. After photo-activation of the diazirine label, the sites of cross-linking to 16S rRNA were identified by our standard procedures. Each of the three tRNA binding sites showed a characteristic pattern of cross-linking. From tRNA at the A site, a major cross-link was observed to position 1378 of the 16S RNA, and a minor one to position 936. From the P site, there were major cross-links to positions 693 and to 957 and/or 966, as well as a minor cross-link to position 1338. The E site bound tRNA showed major cross-links to position 693 (identical to that from the P site) and to positions 1376/1378 (similar, but not identical, to the cross-link observed from the A site). Immunological analysis of the concomitantly cross-linked ribosomal proteins indicated that S7 was the major target of cross-linking from all three tRNA sites, with S11 as a minor product. The results are discussed in terms of the overall topography of the decoding region of the 30S ribosomal subunit. Topics: Anticodon; Azirines; Base Sequence; Binding Sites; Cross-Linking Reagents; Cytidine; Escherichia coli; Models, Genetic; Molecular Sequence Data; Nucleic Acid Conformation; Peptide Chain Elongation, Translational; Ribonuclease H; Ribosomes; RNA, Bacterial; RNA, Messenger; RNA, Ribosomal, 16S; RNA, Transfer, Arg; Transfer RNA Aminoacylation; Ultraviolet Rays	1994
Analysis of modification-dependent structural alterations in the anticodon loop of Escherichia coli tRNAArg and their effects on the translation of MS2 RNA. European journal of biochemistry, 1985, Nov-04, Volume: 152, Issue:3 The conformation of the anticodon loop of Escherichia coli tRNAArg was investigated. It is shown that the structure of the anticodon loop is influenced by the base composition of the anticodon stem, and the natural modification of the nucleoside residue 32 in the anticodon loop. The structural effects detected by analysis of the accessibility of the anticodon loop to nuclease S1 could be correlated with the ability of different Arg-tRNAArg species to suppress frame-shifting during translation of MS2 RNA. Topics: Anticodon; Coliphages; Cytidine; Endonucleases; Escherichia coli; Nucleic Acid Conformation; Protein Biosynthesis; RNA, Transfer; RNA, Transfer, Amino Acyl; RNA, Viral; Single-Strand Specific DNA and RNA Endonucleases	1985

Article

Year

The decoding region of 16S RNA; a cross-linking study of the ribosomal A, P and E sites using tRNA derivatized at position 32 in the anticodon loop.

The EMBO journal, 1994, Jun-01, Volume: 13, Issue:11

A photo-reactive diazirine derivative was attached to the 2-thiocytidine residue at position 32 of tRNA(Arg)I from Escherichia coli. This modified tRNA was bound under suitable conditions to the A, P or E site of E.coli ribosomes. After photo-activation of the diazirine label, the sites of cross-linking to 16S rRNA were identified by our standard procedures. Each of the three tRNA binding sites showed a characteristic pattern of cross-linking. From tRNA at the A site, a major cross-link was observed to position 1378 of the 16S RNA, and a minor one to position 936. From the P site, there were major cross-links to positions 693 and to 957 and/or 966, as well as a minor cross-link to position 1338. The E site bound tRNA showed major cross-links to position 693 (identical to that from the P site) and to positions 1376/1378 (similar, but not identical, to the cross-link observed from the A site). Immunological analysis of the concomitantly cross-linked ribosomal proteins indicated that S7 was the major target of cross-linking from all three tRNA sites, with S11 as a minor product. The results are discussed in terms of the overall topography of the decoding region of the 30S ribosomal subunit.

Topics: Anticodon; Azirines; Base Sequence; Binding Sites; Cross-Linking Reagents; Cytidine; Escherichia coli; Models, Genetic; Molecular Sequence Data; Nucleic Acid Conformation; Peptide Chain Elongation, Translational; Ribonuclease H; Ribosomes; RNA, Bacterial; RNA, Messenger; RNA, Ribosomal, 16S; RNA, Transfer, Arg; Transfer RNA Aminoacylation; Ultraviolet Rays

1994

Analysis of modification-dependent structural alterations in the anticodon loop of Escherichia coli tRNAArg and their effects on the translation of MS2 RNA.

European journal of biochemistry, 1985, Nov-04, Volume: 152, Issue:3

The conformation of the anticodon loop of Escherichia coli tRNAArg was investigated. It is shown that the structure of the anticodon loop is influenced by the base composition of the anticodon stem, and the natural modification of the nucleoside residue 32 in the anticodon loop. The structural effects detected by analysis of the accessibility of the anticodon loop to nuclease S1 could be correlated with the ability of different Arg-tRNAArg species to suppress frame-shifting during translation of MS2 RNA.

Topics: Anticodon; Coliphages; Cytidine; Endonucleases; Escherichia coli; Nucleic Acid Conformation; Protein Biosynthesis; RNA, Transfer; RNA, Transfer, Amino Acyl; RNA, Viral; Single-Strand Specific DNA and RNA Endonucleases

1985