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Oct-1 [corrected] and Oct-2 DNA-binding site specificity is regulated in vitro by different kinases.
- Source :
-
The Biochemical journal [Biochem J] 1996 May 01; Vol. 315 ( Pt 3), pp. 889-93. - Publication Year :
- 1996
-
Abstract
- The transcription factors Oct-1 and Oct-2 bind differentially to three octamer binding sequences corresponding to the octamer binding site from the H2B promoter [ATGCTAATAA], a simple TAATGARAT motif, found in herpes simplex virus IE4/5 genes [GCGGTAATGAGAT], and a perfect consensus overlapping octamer/TAATGARAT motif [ATGCTAATGAGAT]. By comparing the effects of protein kinase A, protein kinase C and casein kinase 2 in vitro on the binding of Oct-1 and Oct-2 to the three motifs, we show that the actions of these kinases regulate Oct-1 and Oct-2 DNA binding independently of each other in a binding-site-specific manner. Inhibition of cellular phosphatases also regulate Oct-1 and Oct-2 DNA binding in a binding-site-specific manner. Both kinase and phosphatase activity are important for regulating the DNA binding activity of Oct-1 and Oct-2 because, in the presence of phosphatase inhibitors, protein kinase A attenuates the binding of both Oct-1 and Oct-2 to the octamer binding site but enhances binding when phosphatase inhibitors are omitted. Thus the DNA specificity of Oct-1 and Oct-2 can be regulated in vitro by the action of different kinases.
- Subjects :
- Base Sequence
Binding Sites
Casein Kinase II
Cell Line
Cyclic AMP-Dependent Protein Kinases metabolism
DNA genetics
DNA-Binding Proteins chemistry
Enzyme Inhibitors pharmacology
Host Cell Factor C1
Humans
In Vitro Techniques
Molecular Sequence Data
Octamer Transcription Factor-1
Octamer Transcription Factor-2
Phosphoric Monoester Hydrolases antagonists & inhibitors
Phosphoric Monoester Hydrolases metabolism
Phosphorylation
Protein Kinase C metabolism
Protein Processing, Post-Translational
Protein Serine-Threonine Kinases metabolism
Transcription Factors chemistry
DNA metabolism
DNA-Binding Proteins metabolism
Transcription Factors metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0264-6021
- Volume :
- 315 ( Pt 3)
- Database :
- MEDLINE
- Journal :
- The Biochemical journal
- Publication Type :
- Academic Journal
- Accession number :
- 8645173
- Full Text :
- https://doi.org/10.1042/bj3150889