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PMID:9659920

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Citation

Simos, G, Sauer, A, Fasiolo, F and Hurt, EC (1998) A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases. Mol. Cell 1:235-42

Abstract

Two yeast enzymes that catalyze aminoacylation of tRNAs, MetRS and GluRS, form a complex with the protein Arc1p. We show here that association of Arc1p with MetRS and GluRS is required in vivo for effective recruitment of the corresponding cognate tRNAs within this complex. Arc1p is linked to MetRS and GluRS through its amino-terminal domain, while its middle and carboxy-terminal parts comprise a novel tRNA-binding domain. This results in high affinity binding of cognate tRNAs and increased aminoacylation efficiency. These findings suggest that Arc1p operates as a mobile, trans-acting tRNA-binding synthetase domain and provide new insight into the role of eukaryotic multimeric synthetase complexes.

Links

PubMed

Keywords

Amino Acyl-tRNA Synthetases/metabolism; Binding Sites/physiology; Conserved Sequence; Fungal Proteins/chemistry; Fungal Proteins/genetics; Genetic Complementation Test; Multienzyme Complexes/metabolism; Mutagenesis/physiology; Protein Structure, Tertiary; RNA, Transfer, Glu/metabolism; RNA, Transfer, Met/metabolism; RNA-Binding Proteins/chemistry; RNA-Binding Proteins/genetics; Saccharomyces cerevisiae Proteins; Yeasts/chemistry; Yeasts/enzymology; Yeasts/genetics

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

YEAST:ARC1

involved_in

GO:0006418: tRNA aminoacylation for protein translation

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

YEAST:ARC1

part_of

GO:0017102: methionyl glutamyl tRNA synthetase complex

ECO:0000315: mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

See also

References

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