Identification of critical residues for G-1 addition and substrate recognition by tRNA(His) guanylyltransferase.

doi:10.1021/bi702517q

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Article

Identification of critical residues for G-1 addition and substrate recognition by tRNA(His) guanylyltransferase.

Biochemistry - 22 Apr 2008

Jackman Jane E, Phizicky Eric M

Abstract excerpt

The yeast tRNA(His) guanylyltransferase (Thg1) is an essential enzyme in yeast. Thg1 adds a single G residue to the 5' end of tRNA(His) (G(-1)), which serves as a crucial determinant for aminoacylation of tRNA(His). Thg1 is the only known gene product that catalyzes the 3'-5' addition of a single nucleotide via a normal phosphodiester bond, and since there is no identifiable sequence similarity between Thg1 and...

Topics

Alanine
Amino Acid Sequence
Humans
Kinetics
Molecular Sequence Data
Mutation
Nucleotidyltransferases
Phosphorylation
RNA, Transfer, His
Saccharomyces cerevisiae
Sequence Alignment
Sequence Homology, Amino Acid
Substrate Specificity

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Open in PubMed

Identifiers

PMID: 18366186
DOI: 10.1021/bi702517q

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