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RNA silencing is one of the important phenomenon in plant defense mechanism, it actively protect host plants against viral infections. Existing viruses must have developed counter defense strategies to survive this arms race. Such counter defense strategy is the viral silencing suppressor (VSRs) which have been reported to directly interfere with the various steps leading to the interference of viral RNAs. Most identified VSRs are multifunctional, besides being RNA-silencing suppressors, they often perform essential roles by functioning as coat proteins, helper components for viral transmission, replicases and movement proteins, proteases or transcriptional regulators. One such identified VSR is AC4 of Sri Lankan cassava mosaic virus strain. Trivial knowledge about the structure –function relationship of this VSR leads to this work, where we focus on the structure generation by modelling to identify the mode of interactions with the various effector molecules of the silencing pathways. Structural analyses have been performed to screen interacting residues. Results indicate conserved structural features which signify propensity of functional interactions and further shows that this VSR can be a potent tool for the analysis of RNA silencing mechanisms and the relationships between different silencing pathways and VSRs.
Incomplete reduction of oxygen molecules is the primary source for the formation of reactive oxygen species (ROS) during cytosolic metabolism or mitochondrial respiration. These phenomenons may be as a result of biotic or abiotic stress. Exposure to exogenous stimuli such as radiation might be an alternative pathway of ROS production. Thus plants require counter defense strategies to combat the increase of this toxic molecular build up in its cell cytoplasm. As a result they have devised an army of free radical scavenging enzymes which enable them to dissipate the oxidative stress imposed by the accumulation of these toxic moieties. Glutathione Peroxidase forms an important part of this arms race along with several catalases and organelle specific enzymes such as superoxide dismutase. Plant glutathione peroxidases(GPXs) have been studied exclusively for their evolutionary lineages since they represent a hybrid class of molecules in context of the presence and absence of selenocysteine at their catalytic centres, the former situation predominant in non vascular plant groups while the later a predominant feature of vascular plants. This analysis focuses on three important aspects of protein structure analyses – hydrophobic cluster analyses for identification of homologues, and acetylation and myristoylation sites which provide us with information regarding the post translational modifications of a particular protein group. Specific patterns of clusters along with acetylation and myristoylation site frequencies were obtained which indicate that GPXs of non vascular plant members possess less chances of getting myristoylated while acetylation was predominant in most land plant lineages but absent in aquatic members.
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