Linked Life Data

2912694

Source:http://linkedlifedata.com/resource/pubmed/id/2912694

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-3-7
pubmed:abstractText
Recently we have purified and characterized a factor in rat liver cytosol that enhances nuclear binding of the activated glucocorticoid-receptor complex in the presence of ATP [an ATP-stimulated translocation promoter (ASTP)]. It has a mol wt of 93,000, S value of 6.5, and pI of 4.5. Here we report studies on the binding of ASTP to histones from calf thymus. Higher salt concentrations were required to disrupt the binding of ASTP to histone-agarose than to disrupt its binding to the anion exchanger diethylaminoethyl-cellulose (half-maximal concentration for inhibition: 200 mM vs. 60 mM KCl). ATP decreased the binding of ASTP to histone-agarose in a dose-dependent fashion, but ADP and AMP had no appreciable effect on the binding. Pyridoxal 5'-phosphate (10 mM) inhibited the binding of ASTP to histone-agarose, whereas 10 mM pyridoxal, pyridoxamine 5'-phosphate, pyridoxamine, and pyridoxine were not inhibitory. ASTP did not bind to histone-agarose that had been pretreated with pyridoxal 5'-phosphate and then reduced with sodium borohydride. In contrast, ASTP pretreated in the same way could bind to histone-agarose. Therefore, modification of lysine residues of histones by pyridoxal 5'-phosphate (Schiff base) presumably inhibited the binding of ASTP to the immobilized histone. Competition experiments with various histones (H1, H2A, H2B, H3, and H4) indicated that ASTP bound to the arginine-rich histones H3 and H4, with preference for H4. These observations together suggest that lysine residues in H4 and H3 are essential for the binding of ASTP to histone. The implications of this interaction are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
124
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
675-80
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Properties of an adenosine triphosphate-stimulated factor that enhances the nuclear binding of activated glucocorticoid-receptor complex: binding to histone-agarose.
pubmed:affiliation
Department of Oncology, Osaka University Medical School, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't