Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5395
pubmed:dateCreated
1998-12-28
pubmed:databankReference
pubmed:abstractText
Early in Drosophila embryogenesis, gap gene products directly repress transcription of homeotic (HOX) genes and thereby delimit HOX expression domains. Subsequently, Polycomb-group proteins maintain this repression. Currently, there is no known molecular link between gap and Polycomb-group proteins. Here, dMi-2 is identified as a protein that binds to a domain in the gap protein Hunchback that is specifically required for the repression of HOX genes. Genetic analyses show that dMi-2 participates in both Hunchback and Polycomb repression in vivo. Hence, recruitment of dMi-2 may serve as a link between repression of HOX genes by Hunchback and Polycomb proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Abd-B proteins, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Polycomb protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/Posterior sex combs protein..., http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Ubx protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/hunchback protein, Drosophila
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
282
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1897-900
pubmed:dateRevised
2008-10-15
pubmed:meshHeading
pubmed-meshheading:9836641-Adenosine Triphosphatases, pubmed-meshheading:9836641-Animals, pubmed-meshheading:9836641-Autoantigens, pubmed-meshheading:9836641-Carrier Proteins, pubmed-meshheading:9836641-DNA-Binding Proteins, pubmed-meshheading:9836641-Drosophila, pubmed-meshheading:9836641-Drosophila Proteins, pubmed-meshheading:9836641-Embryo, Nonmammalian, pubmed-meshheading:9836641-Gene Dosage, pubmed-meshheading:9836641-Gene Expression Regulation, Developmental, pubmed-meshheading:9836641-Genes, Homeobox, pubmed-meshheading:9836641-Genes, Insect, pubmed-meshheading:9836641-Genetic Complementation Test, pubmed-meshheading:9836641-Germ Cells, pubmed-meshheading:9836641-Heterozygote, pubmed-meshheading:9836641-Homeodomain Proteins, pubmed-meshheading:9836641-In Situ Hybridization, pubmed-meshheading:9836641-Insect Proteins, pubmed-meshheading:9836641-Mutation, pubmed-meshheading:9836641-Recombinant Fusion Proteins, pubmed-meshheading:9836641-Transcription Factors
pubmed:year
1998
pubmed:articleTitle
dMi-2, a hunchback-interacting protein that functions in polycomb repression.
pubmed:affiliation
Max-Planck-Institut für Entwicklungsbiologie, Spemannstrasse 35/III, 72076 Tübingen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't