Ontology highlight
ABSTRACT:
SUBMITTER: So BR
PROVIDER: S-EPMC3173103 | biostudies-literature | 2011 Sep
REPOSITORIES: biostudies-literature
So Byung Ran BR An Songon S Kumar Sandeep S Das Mom M Turner Daniel A DA Hadad Christopher M CM Musier-Forsyth Karin K
The Journal of biological chemistry 20110718 36
Aminoacyl-tRNA synthetases attach specific amino acids to cognate tRNAs. Prolyl-tRNA synthetases are known to mischarge tRNA(Pro) with the smaller amino acid alanine and with cysteine, which is the same size as proline. Quality control in proline codon translation is partly ensured by an editing domain (INS) present in most bacterial prolyl-tRNA synthetases that hydrolyzes smaller Ala-tRNA(Pro) and excludes Pro-tRNA(Pro). In contrast, Cys-tRNA(Pro) is cleared by a freestanding INS domain homolog ...[more]