[Interaction of s4U8 region of tRNA Phe with tRNA-(adenine-1-)-methyltransferase from Thermus thermophilus].
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.
Venkstern
T V
TV
Graĭfer
D M
DM
Gracheva
E A
EA
Karpova
G G
GG
Morozov
I A
IA
D003432:Cross-Linking Reagents; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D012345:RNA, Transfer, Amino Acid-Specific / Q000378:metabolism*; D012360:RNA, Transfer, Phe / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D013824:Thermus / Q000201:enzymology*; D012359:tRNA Methyltransferases / Q000378:metabolism*
D003432:Cross-Linking Reagents; D012345:RNA, Transfer, Amino Acid-Specific; D012360:RNA, Transfer, Phe; D012359:tRNA Methyltransferases; C023194:tRNA (adenine(58)-N(1))-methyltransferase
Vzaimodeĭstvie raĭona s4U8 tRNK Phe s tRNK-(adenin-1-)-metil- transferazoĭ iz Thermus thermophilus.