Identity elements of Saccharomyces cerevisiae tRNA(His).
Recognition of tRNA(His) by Saccharomyces cerevisiae histidyl-tRNA synthetase was studied using in vitro transcripts. Histidine tRNA is unique in possessing an extra nucleotide, G-1, at the 5' end. Mutation studies indicate that this irregular secondary structure at the end of the acceptor stem is important for aminoacylation with histidine, while the requirement of either base of this extra base pair is smaller than that in Escherichia coli. The anticodon was also found to be required for histidylation. The regions involved in histidylation are essentially the same as those in E.coli, whereas the proportion of the contributions of the two portions distant from each other, the anticodon and the end of the acceptor stem, makes a substantial difference between the two systems.
Nameki
N
N
Institute of Space and Astronautical Science, Kanagawa, Japan.
Asahara
H
H
Shimizu
M
M
Okada
N
N
Himeno
H
H
D000215:Acylation; D000926:Anticodon / Q000235:genetics*; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D006151:Guanosine / Q000502:physiology; D006643:Histidine-tRNA Ligase / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D009154:Mutation / Q000502:physiology; D009690:Nucleic Acid Conformation; D012354:RNA, Transfer, His / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics*; D013045:Species Specificity
D000926:Anticodon; D012354:RNA, Transfer, His; D006151:Guanosine; D006643:Histidine-tRNA Ligase