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1.
[Mobility of the spin-labeled N-acylaminoacyl residue of N-acyl-phen-tRNAphen in a ribosomal system and in complexes with phen-tRNAphen synthetase]. / Podvizhnost' spin-mechenogo N-atsilaminoatsil'nogo ostatka N-atsil-fen-tRNKfen v ribosomal'noi sisteme i kompleksakh s fen-tRNKfen sintetazoi.
Vosel', S V; Kukina, T P; Popova, V I; Nuzhdina, N A; Lavrik, O I.
Biofizika ; 24(5): 933-4, 1979.
Article in Russian | MEDLINE | ID: mdl-226176

Subject(s)
Amino Acyl-tRNA Synthetases , Phenylalanine-tRNA Ligase , Phenylalanine , RNA, Transfer , Ribosomes/metabolism , Electron Spin Resonance Spectroscopy
2.
[Chemical modification of the complex of tRNA Phe with phenylalanyl-tRNA synthetase from Escherichia coli]. / Issledovanie khimicheskoi modifikatsii kompleksa tRNK s fenilalanil-tRNK-sintetazoi Escherichia coli.
Ankilova, V N; Vlasov, V V; Mamaev, S V; Nuzhdina, N A.
Mol Biol (Mosk) ; 13(5): 994-1000, 1979.
Article in Russian | MEDLINE | ID: mdl-388193

ABSTRACT

Alkylation of E. coli tRNAPhe, bound to the cognate synthetase was investigated. The alkylating reagent is a derivative of 2-chloroethylamine: 2',3'-O-[4(N-2-chloroethyl-N-methylamino)-benzylidene]-uridine-5'-methylphosphate. It was found that the enzyme protects from the reaction D-stem (guanosine G24) and the region of juxtaposition of acceptor stem and D-stem (S4U8 and C13) in the tRNAPhe.


Subject(s)
Amino Acyl-tRNA Synthetases , Escherichia coli/enzymology , Phenylalanine-tRNA Ligase , RNA, Transfer , Alkylation , Amino Acyl-tRNA Synthetases/metabolism , Base Sequence , Nucleic Acid Conformation , Phenylalanine , Phenylalanine-tRNA Ligase/metabolism , Protein Binding
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