Interaction of s4U8 region of tRNA Phe with tRNA- (adenine-1-) -methyltransferase from Thermus thermophilus
Venkstern, T.V.; Graĭfer, D.M.; Gracheva, E.A.; Karpova, G.G.; Morozov, I.A.
Bioorganicheskaia Khimiia 13(10): 1344-1350
1987
ISSN/ISBN: 0132-3423 PMID: 3325064 Document Number: 300367
Photoaffinity labelling of tRNA (adenine-1-)-methyltransferase with an E. coli tRNA(Phe) derivative bearing 4-azidophenylmercuro group attached to s4U residue as well as direct photocross-linking of the native tRNA(Phe) with the enzyme via s4U residue has been studied. Both techniques labelling gave similar results, leading to covalent attachment of tRNA(Phe) to the enzyme within a specific complex. The data obtained indicate unambigously that s4U residue contacts with tRNA (adenine-1-)-methyltransferase within the corresponding specific complex.