Glycosylation of RNA polymerase II from wheat germ
| Autor: | Laura Cervoni, Franco Marmocchi, Anna Ferraro, Carlo Turano, Margherita Eufemi, Patrizia Ciavatta |
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| Rok vydání: | 1997 |
| Předmět: |
Calf thymus
Glycosylation Protein subunit Biophysics RNA polymerase II Thymus Gland Biochemistry chemistry.chemical_compound Structural Biology Genetics Monosaccharide Animals Sugar Molecular Biology Polymerase Triticum Glycoproteins chemistry.chemical_classification biology Galactose Cell Biology Carbohydrate Galactosyltransferases Wheat germ Molecular biology Molecular Weight Enzyme chemistry biology.protein Cattle RNA Polymerase II |
| Zdroj: | FEBS letters. 417(2) |
| ISSN: | 0014-5793 |
| Popis: | RNA polymerase II from wheat germ was analyzed for the presence of sugars. The two largest subunits and the 27 and 25 kDa subunits were found to be glycosylated by a variety of sugars. However, no N-acetylglucosamine was detected, which was found by Kelly et al. (J. Biol. Chem. (1993) 268, 10416–10424) in the largest subunit of RNA polymerase II from calf thymus. Thus it appears that the regulatory function of this sugar, postulated by Kelly et al., is performed in the wheat germ enzyme by other monosaccharides. Carbohydrate analysis of the two largest subunits of the calf thymus enzyme also revealed the presence, beside N-acetylglucosamine, of other sugars. Some similarities in the features of glycosylation of the two polymerases, isolated from very different organisms, suggest that the sugar moieties have an important role in the structure and/or function of these enzymes. |
| Databáze: | OpenAIRE |
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