Nucleotides in yeast tRNAPhe required for the specific recognition by its cognate synthetase.
An analysis of the aminoacylation kinetics of unmodified yeast tRNAPhe mutants revealed that five single-stranded nucleotides are important for its recognition by yeast phenylalanyl-tRNA synthetase, provided they were positioned correctly in a properly folded tRNA structure. When four other tRNAs were changed to have these five nucleotides, they became near-normal substrates for the enzyme.
Sampson
J R
JR
Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.
DiRenzo
A B
AB
Behlen
L S
LS
Uhlenbeck
O C
OC
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D009690:Nucleic Acid Conformation; D010652:Phenylalanine-tRNA Ligase / Q000378:metabolism*; D010944:Plants / Q000235:genetics; D012345:RNA, Transfer, Amino Acid-Specific / Q000235:genetics*; D012360:RNA, Transfer, Phe / Q000235:genetics* / Q000378:metabolism; D012568:Schizosaccharomyces / Q000235:genetics; D014158:Transcription, Genetic; D014908:Triticum / Q000235:genetics
D012345:RNA, Transfer, Amino Acid-Specific; D012360:RNA, Transfer, Phe; D000604:Amino Acyl-tRNA Synthetases; D010652:Phenylalanine-tRNA Ligase