Abstract 2293 Resurrection of ancestral aspartyl-tRNA synthetases

Protein synthesis is essential for life and requires the correct pairing of amino acids to their cognate transfer tRNA by aminoacyl-tRNA synthetases. Many prokaryotes lack an asparaginyl-tRNA synthetase (AsnRS) to directly attach asparagine to its cognate tRNA (tRNAAsn). Instead these organisms use a non-discriminating aspartyl-tRNA synthetase (ND-AspRS) to attach aspartate to tRNAAsn and GatCAB to amidate the aspartate to asparagine. Organisms with an AsnRS often have a discriminating aspartyl-tRNA synthetase (D-AspRS) that only attaches Asp to tRNAAsp in contrast to ND-AspRS being able to use both tRNAAsp and tRNAAsn as substrate.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109651
Primary Topic
RNA and protein synthesis mechanisms
Type
article
Field-Weighted Citation Impact
0.00

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article

Abstract 2293 Resurrection of ancestral aspartyl-tRNA synthetases

Lindsey Han, Kelly Sheppard
Journal of Biological Chemistry
RNA and protein synthesis mechanisms
article

Abstract 2293 Resurrection of ancestral aspartyl-tRNA synthetases

Lindsey Han, Kelly Sheppard
article en

Abstract

Protein synthesis is essential for life and requires the correct pairing of amino acids to their cognate transfer tRNA by aminoacyl-tRNA synthetases. Many prokaryotes lack an asparaginyl-tRNA synthetase (AsnRS) to directly attach asparagine to its cognate tRNA (tRNAAsn). Instead these organisms use a non-discriminating aspartyl-tRNA synthetase (ND-AspRS) to attach aspartate to tRNAAsn and GatCAB to amidate the aspartate to asparagine. Organisms with an AsnRS often have a discriminating aspartyl-tRNA synthetase (D-AspRS) that only attaches Asp to tRNAAsp in contrast to ND-AspRS being able to use both tRNAAsp and tRNAAsn as substrate.

Journal of Biological ChemistryVol. 301(5)
Florida International University (US)
National Science Foundation, National Institutes of Health
Zero hunger
Openalex Percentile: Top 88%
RNA and protein synthesis mechanisms
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