Irreversible inactivation of arginyl-tRNA ligase by periodate-oxidized tRNA
نویسندگان
چکیده
منابع مشابه
L-arginine recognition by yeast arginyl-tRNA synthetase.
The crystal structure of arginyl-tRNA synthetase (ArgRS) from Saccharomyces cerevisiae, a class I aminoacyl-tRNA synthetase (aaRS), with L-arginine bound to the active site has been solved at 2.75 A resolution and refined to a crystallographic R-factor of 19.7%. ArgRS is composed predominantly of alpha-helices and can be divided into five domains, including the class I-specific active site. The...
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Identity determinants are essential for the accurate recognition of transfer RNAs by aminoacyl-tRNA synthetases. To date, arginine determinants in the yeast Saccharomyces cerevisiae have been identified exclusively in vitro and only on a limited number of tRNA Arginine isoacceptors. In the current study, we favor a full cellular approach and expand the investigation of arginine determinants to ...
متن کاملArginyl-tRNA Synthetase Facilitates Complex Formation Between Seryl-tRNA Synthetase and its Cognate Transfer RNA
Several studies have revealed the involvement of multi aminoacyl-tRNA synthetase complexes (MSC) in archaeal and eukaryotic translation. Here we analyzed interactions of atypical Methanothermobacter thermautotrophicus seryl-tRNA synthetase (MtSerRS), transfer RNA (tRNA) and arginyl-tRNA synthetase (ArgRS). Surface plasmon resonance (SPR) was used to determine dissociation constants for the MtSe...
متن کاملStructural and mutational studies of the recognition of the arginine tRNA-specific major identity element, A20, by arginyl-tRNA synthetase.
Arginyl-tRNA synthetase (ArgRS) recognizes two major identity elements of tRNA(Arg): A20, located at the outside corner of the L-shaped tRNA, and C35, the second letter of the anticodon. Only a few exceptional organisms, such as the yeast Saccharomyces cerevisiae, lack A20 in tRNA(Arg). In the present study, we solved the crystal structure of a typical A20-recognizing ArgRS from Thermus thermop...
متن کاملStructure-function analysis of yeast tRNA ligase.
Trl 1 is an essential 827-amino-acid enzyme that executes the end-healing and end-sealing steps of tRNA splicing in Saccharomyces cerevisiae. Trl1 consists of two catalytic domains--an N-terminal adenylyltransferase/ligase component (amino acids 1-388) and a C-terminal 5'-kinase/cyclic phosphodiesterase component (amino acids 389-827)--that can function in tRNA splicing in vivo when expressed a...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1979
ISSN: 0014-5793
DOI: 10.1016/0014-5793(79)80240-9