Identity elements ofSaccharomyces cerevisiaetRNAHis | Zendy

Nobukazu Nameki | Zendy; Haruichi Asahara | Zendy; Mikio Shimizu | Zendy; Norihiro Okada | Zendy; Hyouta Himeno | Zendy

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Identity elements ofSaccharomyces cerevisiaetRNA^His

Author(s) -

Nobukazu Nameki,

Haruichi Asahara,

Mikio Shimizu,

Norihiro Okada,

Hyouta Himeno

Publication year - 1995

Publication title -

nucleic acids research

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/23.3.389

Subject(s) - transfer rna , biology , aminoacylation , saccharomyces cerevisiae , histidine , escherichia coli , base pair , biochemistry , genetics , saccharomyces , mutation , nucleotide , wobble base pair , rna , dna , yeast , enzyme , gene

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.

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