دانلود رایگان مقاله لاتین مدل سازی کلونینگ مولکولی از سایت الزویر
عنوان فارسی مقاله:
مدل سازی کلونینگ مولکولی و همسانی Tyrosylprotein Sulfotransferaseجدید حلزون دریایی
عنوان انگلیسی مقاله:
Molecular Cloning and Homology Modeling of Novel Tyrosylprotein Sulfotransferase of Marine Mollusk
سال انتشار : 2016
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مقدمه انگلیسی مقاله:
1. Introduction
Tyrosylprotein sulfotransferases (TPSTs1 , EC 2.8.2.20) are the Golgi-localized type II transmembrane proteins, which transfer a sulfuryl group (SO3 2−) from the universal sulfate donor 3′-phosphoadenosine-5′-phosphosulfate (PAPS) to the hydroxyl of tyrosine side chain (Lee and Huttner, 1983). Tyrosine sulfation is a common post-translational modification of peptides and proteins. TPST activity has been described in many species of animals and plants (Niehrs and Huttner, 1990; Sane and Baker, 1993; Kasinathan et al., 2005; Nishimura and Naito, 2007; Hanai et al., 2000). In 2012, this enzyme was first discovered in a Gramnegative bacterium (Han et al., 2012), although tyrosine sulfation has not previously been reported in prokaryotes. In spite of the functional importance of these enzymes, almost all known TPSTs are of mammalian origins. Only few enzymes from invertebrates have been described (from nematodes Caenorhabditis elegans and Brugia malayi, insects Culex quinquefasciatus, Drosophila spp., and Anopheles gambiae, sea squirts Ciona intestinalis and Halocynthia roretzi, trematode Schistosoma japonicum, marine mollusk Crassostrea gigas) mainly via cDNA or genome sequencing. The sulfation of biomolecules plays an important role in the metabolism of pro- and eukaryotes. The growing scientific interest in the sulfation of different natural compounds stems from the high biological activities of sulfated derivatives and their role in organisms. The known roles of tyrosine sulfation in mammals are various and multiple, for example maintenance of hemostasis,triggering inflammatory responses, strengthening leucocyte adhesion, defining specificity of chemokine receptors and enhancement of potency of bioactive peptides (Coughtrie et al., 1998; Kehoe and Bertozzi, 2000; Moore, 2003; Seibert and Sakmar, 2008). Marine hydrobionts are extremely rich in sulfated metabolites with diverse biological activities (Kornprobst et al., 1998). Unfortunately, sulfation/desulfation processes are studied considerably less than, for example, phosphorylation. The knowledge about the proteins undergoing sulfation in marine organisms is particularly poor. Frequently enzymes from marine habitats have unique properties; some of them are very useful for biotechnological applications. The enzymes with interesting specificities and high level of activities were found in the digestive glands of Littorina sitkana. Previously we isolated and characterized from this mollusk the enzymes, which catalyze hydrolysis and transformation of carbohydrate-containing natural products. There are alginate lyase (Favorov et al., 1979), two forms of fucoidanases (Kusaykin et al., 2003; Bilan et al., 2005), endo-1,3-β-D-glucanase (Pesentseva et al., 2012), β-D-glucosidase (Pesentseva et al., 2008) and sulfatase (Kusaykin et al., 2006). Herbivorous marine gastropod L. sitkana is widely spread on the coasts of the Pacific and the Atlantic Oceans, and it was interesting to search the TPST gene in this animal. The data of the crystal structure of human tyrosylprotein sulfotransferase-2 (Teramoto et al., 2013) and the homology model for human TPST-1 (Nedumpully-Govindan et al., 2014) will give more information about this enzyme. Thus, the present study was devoted to the search for the tyrosylprotein sulfotransferase gene in the marine gastropod, cloning and sequencing of the cDNA encoding this protein, and 3D-structure homology modeling
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کلمات کلیدی:
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