Plant-specific domains and fragmented sequences imply non-canonical functions in plant aminoacyl-trna synthetases

Yusuke Saga, Moeka Kawashima, Shiho Sakai, Kaori Yamazaki, Misato Kaneko, Moeka Takahashi, Natsuko Sato, Yohei Toyoda, Shohei Takase, Takeshi Nakano, Naoto Kawakami, Tetsuo Kushiro

Research output: Contribution to journalArticlepeer-review

Abstract

Aminoacyl-tRNA synthetases (aaRSs) play essential roles in protein translation. In addition, numerous aaRSs (mostly in vertebrates) have also been discovered to possess a range of non-canonical functions. Very few studies have been conducted to elucidate or characterize non-canonical functions of plant aaRSs. A genome-wide search for aaRS genes in Arabidopsis thaliana revealed a total of 59 aaRS genes. Among them, asparaginyl-tRNA synthetase (AsnRS) was found to possess a WHEP domain inserted into the catalytic domain in a plant-specific manner. This insertion was observed only in the cytosolic isoform. In addition, a long stretch of sequence that exhibited weak homology with histidine ammonia lyase (HAL) was found at the N-terminus of histidyl-tRNA synthetase (HisRS). This HAL-like domain has only been seen in plant HisRS, and only in cytosolic isoforms. Additionally, a number of genes lacking minor or major portions of the full-length aaRS sequence were found. These genes encode 14 aaRS fragments that lack key active site sequences and are likely catalytically null. These identified genes that encode plant-specific additional domains or aaRS fragment sequences are candidates for aaRSs possessing non-canonical functions.

Original languageEnglish
Article number1056
Pages (from-to)1-13
Number of pages13
JournalGenes
Volume11
Issue number9
DOIs
Publication statusPublished - Sep 2020

Keywords

  • Aminoacyl-tRNA synthetase
  • Asparaginyl-tRNA synthetase
  • Histidyl-tRNA synthetase
  • Non-canonical function
  • Plant
  • Species-specific domain

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