Linked Life Data

2905684

Source:http://linkedlifedata.com/resource/pubmed/id/2905684

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12A
pubmed:dateCreated
1989-3-6
pubmed:databankReference
pubmed:abstractText
The octamer motif ATGCAAAT is recognized indistinguishably by two mammalian transcription factors: one that is expressed ubiquitously and referred to here as Oct-1, and another, Oct-2, that is expressed in lymphoid cells. We report the cDNA cloning of the human oct-1 gene, which encodes Oct-1, by screening lambda gt11 recombinant phage in situ for octamer motif-specific DNA binding. One lambda gt11 recombinant expressed a beta-galactosidase-octamer-binding fusion protein with a DNA-binding specificity indistinguishable from human HeLa cell Oct-1 protein. As expected for a ubiquitously expressed protein, Oct-1 mRNA is expressed in all five human and two mouse cell lines tested. Polyclonal rabbit antiserum raised against the beta-galactosidase fusion protein shows that the DNA-binding domains of Oct-1 and Oct-2 proteins are related antigenically. Deletion analysis of the 743-amino-acid-long oct-1 open reading frame shows that the DNA-binding activity lies within a central highly charged domain of 160 amino acids. Comparison of the Oct-1 and Oct-2 sequences reveals that this domain is nearly identical between the two proteins. Highly similar domains are also present in the pituitary-specific transcription factor Pit-1 and the Caenorhabditis elegans unc-86 cell lineage gene product (see Herr et al. 1988). Within this shared POU (Pit-1, Oct-1 and Oct-2, unc-86) domain (pronounced 'pow') lie two subdomains: a POU-related homeo box and a POU-specific box. The Oct-1 protein is unique among the POU-related proteins and other homeo box proteins because it is expressed ubiquitously.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0890-9369
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1582-99
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2905684-Amino Acid Sequence, pubmed-meshheading:2905684-Animals, pubmed-meshheading:2905684-Bacteriophage lambda, pubmed-meshheading:2905684-Base Sequence, pubmed-meshheading:2905684-Binding Sites, pubmed-meshheading:2905684-Cell Line, pubmed-meshheading:2905684-Cloning, Molecular, pubmed-meshheading:2905684-DNA-Binding Proteins, pubmed-meshheading:2905684-Genes, pubmed-meshheading:2905684-Genes, Homeobox, pubmed-meshheading:2905684-Host Cell Factor C1, pubmed-meshheading:2905684-Humans, pubmed-meshheading:2905684-Immunoblotting, pubmed-meshheading:2905684-Lymphoid Tissue, pubmed-meshheading:2905684-Mice, pubmed-meshheading:2905684-Molecular Sequence Data, pubmed-meshheading:2905684-Nuclear Proteins, pubmed-meshheading:2905684-Octamer Transcription Factor-1, pubmed-meshheading:2905684-Recombinant Fusion Proteins, pubmed-meshheading:2905684-Restriction Mapping, pubmed-meshheading:2905684-Transcription Factors, pubmed-meshheading:2905684-beta-Galactosidase
pubmed:year
1988
pubmed:articleTitle
The ubiquitous octamer-binding protein Oct-1 contains a POU domain with a homeo box subdomain.
pubmed:affiliation
Cold Spring Harbor Laboratory, New York 11724.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't