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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.
The cytomegalovirus (CMV) genome encodes four clusters of genes expressed immediately after infection — i.e.: UL36-38, UL122-123, TRS1-IRS1, and US3. The general function of these genes is associated with inhibition of cellular mechanisms of antiviral response. Although several biological processes have been mapped onto specific gene products, the knowledge of the molecular mechanism of their activity remains fragmentary. Here, we report the application of protein structure prediction methods in assigning the function to a glycosylated domain encoded by UL37 of CMV (gpUL37, UL37x3). The discerned similarity clearly points out that this domain represents a novel type of a major histocompatibility complex (MHC)-like protein, and consequently may play a central role in an additional mechanism of escape from antiviral response.
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