Biology subjects

SINGH, S.

Publications and source records attributed to SINGH, S..

3 recordsLinked to original sources

bioRxiv2024

PROTEOME DATA BASED IDENTIFICATION OF POTENTIAL RNAi TARGETS FOR COTTON MEALYBUG (Phenacoccus solenopsis Tinsley) POPULATION MANAGEMENT

Background of the studyPhenacoccus solenopsis Tinsley (Hemiptera: Pseudococcidae), commonly known as cotton mealybug, regarded as an invasive pest worldwide, particularly in the tropics and subtropics. It is one of the major pests of cotton and other commercially important crops. Despite the significant economic losses caused by cotton mealybug the molecular aspects of this insect are under-studied. MethodsIn the present study, proteome data of four different developmental stages of cotton mealybug is generated. Differential expression of proteins (DEPs) was studied among six different groups of which, maximum DEPs (550 up-regulated and 1118 down-regulated) were obtained when the quantifiable proteins of Egg+first nymphal were compared with second nymphal instar (FC [≥] 2, P < 0.05). From this proteomics data fifteen potential target genes were predicted for insect pest management. Further, these fifteen genes were explored and evaluated the for RNAi based pest control and optimisation of dsRNA delivery system in cotton mealybug. The analysis of transient expression of target genes was performed. ResultsThe results signified that dsRNA of Ferritin caused [~]69% mortality hence, could be exploited as a promising candidate gene to design a sustainable method for cotton mealybug management. ConclusionThis study provides an urgently required, alternate green control strategy based on proteomics to identify potential RNAi targets for pest management.

molecular biology↗

bioRxiv2022

UBA52 attunes VDAC1-mediated mitochondrial dysfunction and dopaminergic neuronal death

Mitochondrial homeostasis regulates energy metabolism, calcium buffering, cell function and apoptosis. The present study has been conducted to investigate the implications of ubiquitin-encoding gene UBA52 in mitochondrial physiology. Transient expression of Myc-UBA52 in neurons significantly inhibited the rotenone-induced increase in reactive oxygen species generation, nitrite level and depleted glutathione level. Mass spectrometric and co-immunoprecipitation data suggested the profound interaction of UBA52 with mitochondrial outer membrane channel protein, VDAC1 in both the wild-type and Myc--synuclein overexpressed neuronal cells and in the Parkinsons disease (PD)-specific substantia nigra and striatal region of the rat brain. In vitro ubiquitylation assay revealed that UBA52 participates in the ubiquitylation of VDAC1 through E3 ligase CHIP. Myc-UBA52 overexpression in neurons further improved the mitochondrial functionality and cell viability by preventing the alteration in mitochondrial membrane potential, mitochondrial complex-I activity, translocation of cytochrome-c and p-Nrf2 along with effect on intracellular calcium uptake, thus collectively inhibiting the opening of mitochondrial permeability transition pore. Additionally, Myc-UBA52 expression in neuronal cells offered protection against apoptotic and autophagic cell death. Altogether, our findings delineate functional association between UBA52 and mitochondrial homeostasis, providing new insights into the deterrence of dopaminergic cell death during acute PD pathogenesis.

neuroscience↗

bioRxiv2022

UBA52 is crucial in HSP90 ubiquitylation and neurodegenerative signaling during early phase of Parkinson disease

Protein aggregation is one of the major pathological events in age-related Parkinsons disease (PD) pathology, predominantly regulated by the ubiquitin-proteasome system (UPS). UPS essentially requires core component ubiquitin however, its role in PD pathology is obscure. This study aimed to investigate the role of ubiquitin encoding genes in the early phase of PD pathology. Wild-type human Myc--synuclein transfected neurons, -synuclein-PFFs treated cells, rotenone-induced sporadic models of PD and SNCA C57BL/6J-Tg (Th-SNCA*A30P*A53T)39 Eric/J transgenic mice showed downregulated level of UBA52 in conjunction with significant downregulation of tyrosine hydroxylase (TH) and neuronal death. In silico predictions, mass spectrometric analysis and co-immunoprecipitation findings suggested strong interaction of UBA52 with -synuclein, HSP90 and E3-ubiquitin ligase CHIP, besides its co-localization with -synuclein in the mitochondrion. Next, in vitro ubiquitylation assay indicated an imperative requirement of the lysine-63 residue of UBA52 in CHIP-mediated HSP90 ubiquitylation. Myc-UBA52 expressed neurons exhibited the downregulated -synuclein protein abundance with increased TH and restored proteasome activity during the diseased condition. Furthermore, Myc-UBA52 expression inhibited the augmented HSP90 protein level along with its various client proteins, HSP75 (homologue of HSP90 in mitochondrion) and ER stress-related markers during early PD. Taken together, data highlights the critical role of UBA52 in HSP90 ubiquitylation in parallel to its potential contribution to the modulation of various disease-related neurodegenerative signaling targets during the early phase of PD pathology.

neuroscience↗