Post-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthet...
Post-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthetase from archaea
About this item
Full title
Author / Creator
Publisher
Chichester, UK: John Wiley & Sons, Ltd
Journal title
Language
English
Formats
Publication information
Publisher
Chichester, UK: John Wiley & Sons, Ltd
Subjects
More information
Scope and Contents
Contents
To ensure a high fidelity during translation, threonyl‐tRNA synthetases (ThrRSs) harbor an editing domain that removes noncognate
L
‐serine attached to tRNA
Thr
. Most archaeal ThrRSs possess a unique editing domain structurally similar to
D
‐aminoacyl‐tRNA deacylases (DTDs) found in eubacteria and eukaryotes that specifically rem...
Alternative Titles
Full title
Post-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthetase from archaea
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1560354
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1560354
Other Identifiers
ISSN
0261-4189
E-ISSN
1460-2075
DOI
10.1038/sj.emboj.7601278
