| Full text | |
| Author(s): |
Mohan, Chakravarthi
;
Santos Junior, Celio Dias
;
Chandra, Swarnendu
Total Authors: 3
|
| Document type: | Journal article |
| Source: | ARCHIVES OF PHYTOPATHOLOGY AND PLANT PROTECTION; v. 53, n. 5-6, p. 17-pg., 2020-03-06. |
| Abstract | |
Pathogenesis related 10 (PR10) proteins are small, cytosolic proteins sharing a similar three-dimensional structure and diverse functions. The present study aimed to characterise in silico the PR10.1 protein from Saccharum arundinaceum (SaPR10.1), a wild relative of sugarcane. SaPR10.1 is a hydrophilic small acidic protein (17 kDa) that lacks the P-loop motif presumed to be involved in the RNase activity for some PR-10 proteins. Predictions of a rich secondary structure present in SaPR10.1 led us to a protein model that suggests SaPR10.1 can bind to more than one molecule of trans-zeatin using molecular docking. This finding suggests that SaPR10.1, differently from the orthologs, can be involved in more efficient depletion of free trans-zeatin. This idea is reinforced by the phylogenetic analysis, which showed both variants SaPR10 and SaPR10.1 closely related to other monocot species like sorghum, maize, and broomcorn millet and not to wheat. (AU) | |
| FAPESP's process: | 15/10855-9 - Development of transgenic sugarcane more resistant to Sphenophorus levis |
| Grantee: | Chakravarthi Mohan |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |