Linked Life Data

2170018

Source:http://linkedlifedata.com/resource/pubmed/id/2170018

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-11-9
pubmed:abstractText
Efficient transcription of SV40 early genes requires transcription factor Sp1. Here, we report that SV40 infection induces Sp1 phosphorylation. While characterizing this modification, we discovered that Sp1 becomes quantitatively phosphorylated in an in vitro transcription extract. Multiple processive phosphorylation of Sp1 depends on binding of Sp1 to GC box-containing DNA. Cell fractionation and column chromatography reveal that the Sp1 kinase is a nuclear DNA binding protein that corresponds to a previously identified DNA-dependent protein kinase. Because only some trans-activators are phosphorylated by this kinase, Sp1 belongs to a specific subgroup of factors that are phosphorylated upon binding to promoter sequences. Finally, efficient phosphorylation of Sp1 requires both a functional DNA binding domain and a region containing the transcriptional activation domains. Coupling of phosphorylation to DNA binding may represent a novel mechanism for regulating transcriptional initiation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
155-65
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
GC box binding induces phosphorylation of Sp1 by a DNA-dependent protein kinase.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley 94720.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't