Linked Life Data

12130631

Source:http://linkedlifedata.com/resource/pubmed/id/12130631

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
2002-9-2
pubmed:abstractText
Mutations at the Drosophila melanogaster brainiac locus lead to defective formation of the follicular epithelium during oogenesis and to neural hyperplasia. The brainiac gene encodes a type II transmembrane protein structurally similar to mammalian beta1,3-glycosyltransferases. We have cloned the brainiac gene from D. melanogaster genomic DNA and expressed it as a FLAG-tagged recombinant protein in Sf9 insect cells. Glycosyltransferase assays showed that brainiac is capable of transferring N-acetylglucosamine (GlcNAc) to beta-linked mannose (Man), with a marked preference for the disaccharide Man(beta1,4)Glc, the core of arthro-series glycolipids. The activity of brainiac toward arthro-series glycolipids was confirmed by showing that the enzyme efficiently utilized glycolipids from insects as acceptors whereas it did not with glycolipids from mammalian cells. Methylation analysis of the brainiac reaction product revealed a beta1,3 linkage between GlcNAc and Man, proving that brainiac is a beta1,3GlcNAc-transferase. Human beta1,3GlcNAc-transferases structurally related to brainiac were unable to transfer GlcNAc to Man(beta1,4)Glc-based acceptor substrates and failed to rescue a homozygous lethal brainiac allele, indicating that these proteins are paralogous and not orthologous to brainiac.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
32417-20
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12130631-Acetylglucosamine, pubmed-meshheading:12130631-Animals, pubmed-meshheading:12130631-Cell Line, pubmed-meshheading:12130631-Chromatography, High Pressure Liquid, pubmed-meshheading:12130631-Chromatography, Thin Layer, pubmed-meshheading:12130631-Cloning, Molecular, pubmed-meshheading:12130631-Drosophila Proteins, pubmed-meshheading:12130631-Drosophila melanogaster, pubmed-meshheading:12130631-Genetic Complementation Test, pubmed-meshheading:12130631-Glycolipids, pubmed-meshheading:12130631-Humans, pubmed-meshheading:12130631-Membrane Proteins, pubmed-meshheading:12130631-Mutation, pubmed-meshheading:12130631-N-Acetylglucosaminyltransferases, pubmed-meshheading:12130631-Phenotype, pubmed-meshheading:12130631-Signal Transduction, pubmed-meshheading:12130631-Substrate Specificity
pubmed:year
2002
pubmed:articleTitle
The Drosophila melanogaster brainiac protein is a glycolipid-specific beta 1,3N-acetylglucosaminyltransferase.
pubmed:affiliation
Institute of Physiology, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't