Glycosylation of RNA polymerase II from wheat germ
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, 10416–104...
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| Veröffentlicht in: | FEBS letters 1997-11, Vol.417 (2), p.227-230 |
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| creator | Cervoni, Laura Turano, Carlo Ferraro, Anna Ciavatta, Patrizia Marmocchi, Franco Eufemi, Margherita |
| description | 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. |
| doi_str_mv | 10.1016/S0014-5793(97)01285-4 |
| format | Article |
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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
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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.</description><subject>Animals</subject><subject>Calf thymus</subject><subject>Cattle</subject><subject>Galactose - metabolism</subject><subject>Galactosyltransferases - metabolism</subject><subject>Glycoproteins - metabolism</subject><subject>Glycosylation</subject><subject>Molecular Weight</subject><subject>RNA polymerase II</subject><subject>RNA Polymerase II - metabolism</subject><subject>Thymus Gland - enzymology</subject><subject>Triticum - enzymology</subject><subject>Wheat germ</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMtOwzAQRS0EgvL4BKSsECwCdvxeoVIVqIRAAvaWY08gKKmL3VLl70kf6hZWo5l7587oIHRO8DXBRNy8YUxYzqWml1peYVIonrM9NCBK0pwyofbRYGc5QscpfeG-V0QfokNNNaeYDFDx0HQupK6x8zpMs1Blr8_DbBaaroVoE2STSVbF0GbLT7Dz7ANie4oOKtskONvWE_R-P34fPeZPLw-T0fApdxxTlhNPpdJSKV6qkhAhmWcA3pPKcoWlV8rzonSiwEIJZjmtoHSUUy8LL62iJ-hiEzuL4XsBaW7aOjloGjuFsEhGasZEoYs_jUQwSpTAvZFvjC6GlCJUZhbr1sbOEGxWTM2aqVkBM1qaNVPD-r3z7YFF2YLfbW0h9vrjRl_WDXT_CzX347tirawELdfj1anbTRT0YH9qiCa5GqYOfB3BzY0P9R_P_gJkoZfT</recordid><startdate>19971110</startdate><enddate>19971110</enddate><creator>Cervoni, Laura</creator><creator>Turano, Carlo</creator><creator>Ferraro, Anna</creator><creator>Ciavatta, Patrizia</creator><creator>Marmocchi, Franco</creator><creator>Eufemi, Margherita</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>19971110</creationdate><title>Glycosylation of RNA polymerase II from wheat germ</title><author>Cervoni, Laura ; Turano, Carlo ; Ferraro, Anna ; Ciavatta, Patrizia ; Marmocchi, Franco ; Eufemi, Margherita</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5034-1d37897885b8b11674d4eedd1fa5807d88d52bc6206864a53febc353d72d7a83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Calf thymus</topic><topic>Cattle</topic><topic>Galactose - metabolism</topic><topic>Galactosyltransferases - metabolism</topic><topic>Glycoproteins - metabolism</topic><topic>Glycosylation</topic><topic>Molecular Weight</topic><topic>RNA polymerase II</topic><topic>RNA Polymerase II - metabolism</topic><topic>Thymus Gland - enzymology</topic><topic>Triticum - enzymology</topic><topic>Wheat germ</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cervoni, Laura</creatorcontrib><creatorcontrib>Turano, Carlo</creatorcontrib><creatorcontrib>Ferraro, Anna</creatorcontrib><creatorcontrib>Ciavatta, Patrizia</creatorcontrib><creatorcontrib>Marmocchi, Franco</creatorcontrib><creatorcontrib>Eufemi, Margherita</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cervoni, Laura</au><au>Turano, Carlo</au><au>Ferraro, Anna</au><au>Ciavatta, Patrizia</au><au>Marmocchi, Franco</au><au>Eufemi, Margherita</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glycosylation of RNA polymerase II from wheat germ</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1997-11-10</date><risdate>1997</risdate><volume>417</volume><issue>2</issue><spage>227</spage><epage>230</epage><pages>227-230</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>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
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| ispartof | FEBS letters, 1997-11, Vol.417 (2), p.227-230 |
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| source | Wiley-Blackwell Journals; MEDLINE; Elsevier ScienceDirect Journals Complete; Wiley Online Library Free Content; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Animals Calf thymus Cattle Galactose - metabolism Galactosyltransferases - metabolism Glycoproteins - metabolism Glycosylation Molecular Weight RNA polymerase II RNA Polymerase II - metabolism Thymus Gland - enzymology Triticum - enzymology Wheat germ |
| title | Glycosylation of RNA polymerase II from wheat germ |
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