Disease surveillance and farmers' knowledge ofBrachiaria(Syn.Urochloa)grass diseases in Rwanda
AFRICAN JOURNAL OF RANGE & FORAGE SCIENCE
Authors: Uzayisenga, Bellancile; Mutimura, Mupenzi; Muthomi, James W.; Mwang'ombe, Agnes W.; Ghimire, Sita R.
Abstract
Brachiaria(syn.Urochloa) is one of the most important tropical forages grass of African origin. Its performance is affected by different constraints, including diseases. This study assessed the distribution, incidence and severity ofBrachiariadiseases and documented farmers' knowledge onBrachiariadiseases in Rwanda. Surveys were conducted in five districts in the dry and wet seasons of 2018 and 2019. Fungi associated with major diseases were isolated and identified based on internal transcribed spacer sequences. The demographic information and farmers' knowledge ofBrachiariadiseases and yield loss were collected using structured questionnaire. Surveys revealed widespread distribution of leaf blight, leaf rust and leaf spot diseases in Rwanda. Incidence and severity of these diseases differed significantly by districts, seasons and district x season interactions; the exception was the non-significant effect of season and district x season interactions on rust incidence in 2018. Molecular identification revealedPhakopsora apodaas a provisional leaf rust pathogen, and frequent association of fungiEpicoccumspp. andNigrosporaspp. with leaf blight, andBipolaris secalisandFusariumspp. with leaf spot symptoms. This study provides baseline information for future studies onBrachiariadiseases and recognises diseases as a major challenge to sustainable production ofBrachiariagrass in Rwanda and East Africa.
The SUMO Conjugase Ubc9 Protects Dopaminergic Cells from Cytotoxicity and Enhances the Stability of alpha-Synuclein in Parkinson's Disease Models
ENEURO
Authors: Verma, Dinesh Kumar; Ghosh, Anurupa; Ruggiero, Lindsey; Cartier, Etienne; Janezic, Eric; Williams, Dionne; Jung, Eui-Gil; Moore, Michael; Seo, Jong Bok; Kim, Yong-Hwan
Abstract
Small ubiquitin-like modifier (SUMO) is a widespread regulatory mechanism of post-translational modification (PTM) that induces rapid and reversible changes in protein function and stability. Using SUMO conjugase Ubc9-overexpressing or knock-down cells in Parkinson's disease (PD) models, we demonstrate that SUMOylation protects dopaminergic cells against MPP+ or preformed fibrils (PFFs) of alpha-synuclein (alpha-syn)-induced toxicities in cell viability and cytotoxicity assays. In the mechanism of protection, Ubc9 overexpression significantly suppressed the MPP+ or PFF-induced reactive oxygen species (ROS) generation, while Ubc9-RNAi enhanced the toxicity-induced ROS production. Further, PFF-mediated protein aggregation was exacerbated by Ubc9-RNAi in thioflavin T staining, compared with NC1 controls. In cycloheximide (Chx)-based protein stability assays, higher protein level of alpha-syn was identified in Ubc9-enhanced green fluorescent protein (EGFP) than in EGFP cells. Since there was no difference in endogenous mRNA levels of alpha-syn between Ubc9 and EGFP cells in quantitative real-time PCR (qRT-PCR), we assessed the mechanisms of SUMO-mediated delayed alpha-syn degradation via MG132, proteasomal inhibitor, and PMA, lysosomal degradation inducer. Ubc9-mediated SUMOylated alpha-syn avoided PMA-induced lysosomal degradation because of its high solubility. Our results suggest that Ubc9 enhances the levels of SUMO1 and ubiquitin on alpha-syn and interrupts SUMO1 removal from alpha-syn. In immunohistochemistry, dopaminergic axon tips in the striatum and cell bodies in the substantia nigra from Ubc9-overexpressing transgenic mice were protected from MPTP toxicities compared with wild-type (WT) siblings. Our results support that SUMOylation can be a regulatory target to protect dopaminergic neurons from oxidative stress and protein aggregation, with the implication that high levels of SUMOylation in dopaminergic neurons can prevent the pathologic progression of PD.