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A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases.

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.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Simos G,Sauer A,Fasiolo F,Hurt EC

doi

10.1016/s1097-2765(00)80024-6

subject

Has Abstract

pub_date

1998-01-01 00:00:00

pages

235-42

issue

2

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(00)80024-6

journal_volume

1

pub_type

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