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dc.contributor.authorBerninsone, Patricia
dc.contributor.authorLin, Zhen-Yuan
dc.contributor.authorKempner, Ellis S.
dc.contributor.authorHirschberg, Carlos B.
dc.date2022-08-11T08:10:04.000
dc.date.accessioned2022-08-23T16:54:16Z
dc.date.available2022-08-23T16:54:16Z
dc.date.issued1995-06-16
dc.date.submitted2008-08-15
dc.identifier.citation<p>J Biol Chem. 1995 Jun 16;270(24):14564-7.</p>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.270.24.14564
dc.identifier.pmid7540172
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42461
dc.description.abstractThe Golgi lumenal GDPase plays an important role in the mannosylation of proteins and lipids of Saccharomyces cerevisiae by regulating the amount of GDP-mannose available in the Golgi lumen. The enzyme makes available GMP as an antiporter to be coupled with entry of GDP-mannose into the Golgi lumen from the cytosol. Using radiation inactivation and target analysis, we have now determined the functional molecular mass of the GDPase within the Golgi membrane and whether or not the enzyme has functional associations with other Golgi membrane proteins, including mannosyltransferases and the GDP-mannose transporter. The functional size of the GDPase was found to be approximately twice the estimated structural target size of the protein; this strongly suggests that the GDPase protein in situ functions as homodimer and does not require association with other membrane proteins for its function.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=7540172&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1074/jbc.270.24.14564
dc.subjectCarrier Proteins
dc.subjectGlycosylation
dc.subjectGolgi Apparatus
dc.subjectGuanosine Diphosphate Mannose
dc.subjectIntracellular Membranes
dc.subjectMannosyltransferases
dc.subjectPyrophosphatases
dc.subjectSaccharomyces cerevisiae
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleRegulation of yeast Golgi glycosylation. Guanosine diphosphatase functions as a homodimer in the membrane
dc.typeArticle
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume270
dc.source.issue24
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/808
dc.identifier.contextkey579693
html.description.abstract<p>The Golgi lumenal GDPase plays an important role in the mannosylation of proteins and lipids of Saccharomyces cerevisiae by regulating the amount of GDP-mannose available in the Golgi lumen. The enzyme makes available GMP as an antiporter to be coupled with entry of GDP-mannose into the Golgi lumen from the cytosol. Using radiation inactivation and target analysis, we have now determined the functional molecular mass of the GDPase within the Golgi membrane and whether or not the enzyme has functional associations with other Golgi membrane proteins, including mannosyltransferases and the GDP-mannose transporter. The functional size of the GDPase was found to be approximately twice the estimated structural target size of the protein; this strongly suggests that the GDPase protein in situ functions as homodimer and does not require association with other membrane proteins for its function.</p>
dc.identifier.submissionpathoapubs/808
dc.contributor.departmentDepartment of Biochemistry and Molecular Biology
dc.source.pages14564-7


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