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Plant-Specific Domains and Fragmented Sequences Imply Non-Canonical Functions in Plant Aminoacyl-tRNA Synthetases.
- Source :
-
Genes [Genes (Basel)] 2020 Sep 07; Vol. 11 (9). Date of Electronic Publication: 2020 Sep 07. - Publication Year :
- 2020
-
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.
- Subjects :
- Amino Acyl-tRNA Synthetases genetics
Arabidopsis genetics
Arabidopsis growth & development
Arabidopsis Proteins genetics
Aspartate-tRNA Ligase genetics
Catalytic Domain
Histidine-tRNA Ligase genetics
Protein Biosynthesis
RNA, Transfer, Amino Acyl genetics
Amino Acyl-tRNA Synthetases metabolism
Arabidopsis enzymology
Arabidopsis Proteins metabolism
Aspartate-tRNA Ligase metabolism
Genome, Plant
Histidine-tRNA Ligase metabolism
RNA, Transfer, Amino Acyl metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2073-4425
- Volume :
- 11
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Genes
- Publication Type :
- Academic Journal
- Accession number :
- 32906706
- Full Text :
- https://doi.org/10.3390/genes11091056