We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Transcriptional expression of aminoacyl tRNA synthetase genes of Xanthomonas oryzae pv. oryzae (Xoo) on rice-leaf extract treatment and crystal structure of Xoo glutamyl-tRNA synthetase.
- Authors
Thien-Hoang Ho; Myoung-Ki Hong; Seunghwan Kim; Jeong-Gu Kim; Jongha Lee; Kyoungho Jung; Inho Lee; Munyoung Choi; Hyunjae Park; Sanghee Lee; Yeh-Jin Ahn; Lin-Woo Kang
- Abstract
Xanthomonas oryzae pv. oryzae (Xoo) is the causal agent of bacterial blight of rice, one of the most devastating rice diseases. We analysed the time-resolved transcriptional expression of aminoacyl-tRNA synthetase (aaRS) genes in Xoo cells treated with rice-leaf extract. Most aaRS genes showed decreased expression in the initial 30 min and recovered or increased expression in the later 30 min. The protein-synthetic machinery of bacterial cells is an important target for developing antibiotic agents; aaRSs play an essential role in peptide synthesis by attaching amino acids onto the corresponding tRNA. In bacteria, glutaminyl-tRNA (Gln-tRNAGln) is synthesised in two steps by glutamyl-tRNA synthetase (GluRS) and tRNA-dependent aminotransferase, the indirect biosynthetic mechanism of which is not present in eukaryotes. We determined the crystal structure of GluRS from Xoo (XoGluRS) at resolution of 3.0 Å, this being the first GluRS structure from a plant pathogen such as Xoo. The XoGluRS structure consists of five domains, which are conserved in other bacterial GluRS structures. In the bacterial GluRS structures, the Rossmann-fold catalytic domain and the stem-contact domain are most conserved in both sequence and structure. The anticodon-binding domain 1 is less conserved in sequence but overall structure is conserved. The connective-polypeptide domain and the anticodon-binding domain 2 show various conformations in structure. The XoGluRS structure could provide useful information to develop a new pesticide against Xoo and bacterial blight.
- Subjects
RICE bacterial leaf blight; AMINOACYL-tRNA; GLUTAMYL-tRNA synthetase
- Publication
Crop & Pasture Science, 2017, Vol 68, Issue 5, p434
- ISSN
1836-0947
- Publication type
Article
- DOI
10.1071/CP16435