Linked Life Data

1847997

Source:http://linkedlifedata.com/resource/pubmed/id/1847997

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-4-9
pubmed:abstractText
The EBV transactivator protein BZLF1 can bind many sites in the EBV genome, most of which have homology to a consensus AP-1 site, the binding site for the fos/jun family of transcription factors. Here we present evidence that BZLF1 can also recognise the binding site for the CCAAT/enhancer binding protein C/EBP and that a BZLF1 binding site within the BZLF1 promoter is recognised by the C/EBP protein. Analysis of the BZLF1 DNA binding domain suggests that the BZLF1 protein binds to DNA as a dimer using sequences adjacent to a basic DNA binding motif. The BZLF1 dimerisation domain does not have a heptad repeat of leucine residues common to leucine zipper proteins but does have characteristics of a coiled coil structure, as judged by site directed mutagenesis. We therefore propose that the dimerisation domain of BZLF1 is structurally related to the coiled coil structure of leucine zippers but lacks the highly conserved leucine repeat. We show that the PZLF1 dimerisation domain has residues in common with the C/EBP leucine zipper and discuss the possible implications of this relationship.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
195-204
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:1847997-Amino Acid Sequence, pubmed-meshheading:1847997-Binding Sites, pubmed-meshheading:1847997-CCAAT-Enhancer-Binding Proteins, pubmed-meshheading:1847997-DNA, pubmed-meshheading:1847997-DNA-Binding Proteins, pubmed-meshheading:1847997-Herpesvirus 4, Human, pubmed-meshheading:1847997-Leucine Zippers, pubmed-meshheading:1847997-Molecular Sequence Data, pubmed-meshheading:1847997-Nuclear Proteins, pubmed-meshheading:1847997-Promoter Regions, Genetic, pubmed-meshheading:1847997-Proto-Oncogene Proteins, pubmed-meshheading:1847997-Proto-Oncogene Proteins c-fos, pubmed-meshheading:1847997-Repetitive Sequences, Nucleic Acid, pubmed-meshheading:1847997-Sequence Homology, Nucleic Acid, pubmed-meshheading:1847997-Trans-Activators, pubmed-meshheading:1847997-Transcription Factors, pubmed-meshheading:1847997-Viral Proteins
pubmed:year
1991
pubmed:articleTitle
The BZLF1 protein of EBV has a coiled coil dimerisation domain without a heptad leucine repeat but with homology to the C/EBP leucine zipper.
pubmed:affiliation
Department of Pathology, University of Cambridge Addenbrooke's Hospital, London, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't