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Pubmed ID :28362257
Publication Date : //

Role of D-aminoacyl-tRNA deacylase beyond chiral proofreading as a cellular defense against glycine mischarging by AlaRS.


Strict L-chiral rejection through Gly-Pro motif during chiral proofreading underlies the inability of D-aminoacyl-tRNA deacylase (DTD) to discriminate between D-amino acids and achiral glycine. The consequent Gly-tRNA 'misediting paradox' is resolved by EF-Tu in the cell. Here, we show that DTD's active site architecture can efficiently edit mischarged Gly-tRNA species four orders of magnitude more efficiently than even AlaRS, the only ubiquitous cellular checkpoint known for clearing the error. Also, DTD knockout in AlaRS editing-defective background causes pronounced toxicity in even at low-glycine levels which is alleviated by alanine supplementation. We further demonstrate that DTD positively selects the universally invariant tRNA-specific G3•U70. Moreover, DTD's activity on non-cognate Gly-tRNA is conserved across all bacteria and eukaryotes, suggesting DTD's key cellular role as a glycine deacylator. Our study thus reveals a hitherto unknown function of DTD in cracking the universal mechanistic dilemma encountered by AlaRS, and its physiological importance.

Authors : Pawar Komal Ishwar , Suma Katta , Seenivasan Ayshwarya , Kuncha Santosh Kumar , Routh Satya Brata , Kruparani Shobha P , Sankaranarayanan Rajan ,

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EIAAB40678 Aars2,Alanine--tRNA ligase,Alanyl-tRNA synthetase, mitochondrial,AlaRS,Rat,Rattus norvegicus,rCG_43500
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EIAAB40677 AARS2,AARSL,Alanine--tRNA ligase,Alanyl-tRNA synthetase, mitochondrial,AlaRS,Homo sapiens,Human,KIAA1270
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