Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1996-12-9
pubmed:abstractText
All isoforms of the Wilms' tumour suppressor protein, WT1, contain four consecutive zinc fingers which facilitate DNA binding. The predominant WT1 transcript contains a 9 base pair insertion resulting in an additional three amino acids, lysine-threonine-serine (KTS), between zinc fingers 3 and 4. WT1 zinc fingers 2, 3 and 4 are highly homologous to the zinc fingers of the early growth response gene, EGR1. However, only WT1--KTS is capable of binding an EGR1 consensus site. In contrast, the previously described genomic fragment, +P5 (D1S3309E), is bound by both WT1--KTS and WT1 + KTS. In this study, the region within + P5 to which both WT1 -- KTS and WT1 + KTS bind was defined as 5'-GGAGAGGGAGGATC-3'. EGR1 did not bind + P5. By creating zinc finger deletions, we demonstrate that zinc finger 1, but not zinc finger 4, is critical for + P5 binding; whereas zinc finger 4, but not 1, is necessary for the binding of WT1 target sites within EGR1, PDGF A chain and IGF2 promoters. Thus, zinc finger usage can vary with target and + P5 may represent a novel type of WT1 binding site, the physiological relevance of which must be investigated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1461-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
A novel target for the Wilms' tumour suppressor protein (WT1) is bound by a unique combination of zinc fingers.
pubmed:affiliation
Centre for Molecular and Cellular Biology, University of Queensland, St. Lucia, Brisbane, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't