Ontology highlight
ABSTRACT:
SUBMITTER: Kuncha SK
PROVIDER: S-EPMC6097841 | biostudies-literature | 2018 Aug
REPOSITORIES: biostudies-literature
Kuncha Santosh Kumar SK Suma Katta K Pawar Komal Ishwar KI Gogoi Jotin J Routh Satya Brata SB Pottabathini Sambhavi S Kruparani Shobha P SP Sankaranarayanan Rajan R
eLife 20180809
D-aminoacyl-tRNA deacylase (DTD) acts on achiral glycine, in addition to D-amino acids, attached to tRNA. We have recently shown that this activity enables DTD to clear non-cognate Gly-tRNA<sup>Ala</sup> with 1000-fold higher efficiency than its activity on Gly-tRNA<sup>Gly</sup>, indicating tRNA-based modulation of DTD (Pawar et al., 2017). Here, we show that tRNA's discriminator base predominantly accounts for this activity difference and is the key to selection by DTD. Accordingly, the uracil ...[more]