Linked Life Data

10069392

Source:http://linkedlifedata.com/resource/pubmed/id/10069392

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-4-13
pubmed:abstractText
OTX2, a homeodomain protein essential in mouse for the development of structures anterior to rhombomere 3, binds with high affinity to a DNA element (called OTS) present in the human tenascin-C promoter. Here we investigate the binding properties of the full length recombinant human OTX2 and of several deletion mutants to the OTS element. We demonstrate that, upon binding of the protein to its DNA target site, a second molecule of OTX2 is recruited to the complex and that a nearby second binding site is not necessary for this interaction. OTX2 sequences located within a region carboxyl-terminal to the homeodomain are necessary in addition to the homeodomain for binding to DNA. Furthermore, OTX2 dimerization requires the same protein domains necessary for DNA binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
445
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
160-4
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Binding properties of the human homeodomain protein OTX2 to a DNA target sequence.
pubmed:affiliation
Immunobiology Laboratory, IST-National Institute for Cancer Research, Advanced Biotechnology Center, Genova, Italy. briata@sirio.cba.unige.it
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't