Linked Life Data

2121606

Source:http://linkedlifedata.com/resource/pubmed/id/2121606

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1990-12-19
pubmed:abstractText
We report the isolation and characterization of cDNA clones that encode a protein with the same DNA binding specificity as the immunoglobulin heavy chain enhancer binding protein E (muEBP-E). We call the gene encoding this protein Ig/EBP-1. A fusion protein encoded by the cDNA binds specifically to muEBP-E-binding sites (E sites) in both the IgH enhancer and the VH1 promoter. Sequence analysis reveals that Ig/EBP-1 is a member of the "basic-zipper" family of DNA-binding proteins that are characterized by basic regions and heptad repeats of leucine residues. Among known family members, Ig/EBP-1 demonstrates highest homology to C/EBP throughout the DNA-binding domain and leucine repeat region. Ig/EBP-1 and C/EBP have highly overlapping binding specificities; both cloned proteins bind to the IgH enhancer and the VH1 promoter E sites, and Ig/EBP-1 binds to previously characterized C/EBP binding sites in the Rous sarcoma virus (RSV) LTR and the murine albumin promoter. Consistent with their homology in the leucine repeat region, Ig/EBP-1 and C/EBP form heterodimers; Ig/EBP-1 is the first member of this family that has been found to heterodimerize with the well-characterized C/EBP. Ig/EBP-1 mRNA is present in all tissues and cell lines examined, although its levels vary almost 20-fold from different sources, with highest levels in early B cells. In tissues where Ig/EBP-1 and C/EBP are both present, heterodimers may be functionally important. The presence of Ig/EBP-1 in fibroblasts and other tissues where C/EBP is not expressed suggests that Ig/EBP-1 may be functionally important for the activity of the RSV enhancer in these cell types. Finally, elevated expression of Ig/EBP-1 in early B cells may explain in part the enhancer-independent activity of VH promoters early in B-cell development.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0890-9369
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:geneSymbol
Ig/EBP-1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1404-15
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:2121606-Amino Acid Sequence, pubmed-meshheading:2121606-Animals, pubmed-meshheading:2121606-Base Sequence, pubmed-meshheading:2121606-Binding, Competitive, pubmed-meshheading:2121606-CCAAT-Enhancer-Binding Proteins, pubmed-meshheading:2121606-Cloning, Molecular, pubmed-meshheading:2121606-DNA, pubmed-meshheading:2121606-DNA-Binding Proteins, pubmed-meshheading:2121606-Enhancer Elements, Genetic, pubmed-meshheading:2121606-Gene Expression, pubmed-meshheading:2121606-Genes, Immunoglobulin, pubmed-meshheading:2121606-Immunoglobulin Heavy Chains, pubmed-meshheading:2121606-Leucine Zippers, pubmed-meshheading:2121606-Mice, pubmed-meshheading:2121606-Molecular Sequence Data, pubmed-meshheading:2121606-NF-kappa B, pubmed-meshheading:2121606-Nuclear Proteins, pubmed-meshheading:2121606-Promoter Regions, Genetic, pubmed-meshheading:2121606-Regulatory Sequences, Nucleic Acid, pubmed-meshheading:2121606-Sequence Homology, Nucleic Acid
pubmed:year
1990
pubmed:articleTitle
Ig/EBP-1: a ubiquitously expressed immunoglobulin enhancer binding protein that is similar to C/EBP and heterodimerizes with C/EBP.
pubmed:affiliation
Department of Biological Chemistry, University of California, Los Angeles.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.