Evidence for interaction of an aminoacyl transfer RNA synthetase with a region important for the identity of its cognate transfer RNA.
Recent experiments showed that a single base pair (G3:U70) in the amino acid acceptor helix is a major determinant for the identity of Escherichia coli alanine transfer RNA. Experiments reported here show that bound alanine tRNA synthetase protects (from ribonuclease attack) seven consecutive phosphodiester linkages on the 3'-side of the acceptor-T psi C helix (phosphates 65-71) and a few additional sites that are in scattered locations. There is no evidence for interaction of the enzyme with the anticodon, a sequence which can be varied without effect on recognition by alanine tRNA synthetase.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D000818:Animals; D000926:Anticodon; D002417:Cattle; D004926:Escherichia coli / Q000235:genetics; D006863:Hydrogen-Ion Concentration; D009690:Nucleic Acid Conformation; D012344:RNA, Transfer, Ala / Q000378:metabolism*; D012345:RNA, Transfer, Amino Acid-Specific / Q000378:metabolism*; D012355:RNA, Transfer, Ile / Q000378:metabolism; D012259:Ribonuclease, Pancreatic / Q000378:metabolism
D000926:Anticodon; D012344:RNA, Transfer, Ala; D012345:RNA, Transfer, Amino Acid-Specific; D012355:RNA, Transfer, Ile; D012259:Ribonuclease, Pancreatic; D000604:Amino Acyl-tRNA Synthetases