A novel nuclear inhibitor I-92 regulates DNA binding activity of octamer binding protein p92 during the cell cycle
Open Access
- 1 January 1991
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 19 (20) , 5725-5730
- https://doi.org/10.1093/nar/19.20.5725
Abstract
Nuclear DNA binding protein p92 is a sequence specific octamer binding protein with identical molecular weight as the ubiquitous octamer binding protein Oct-1. It binds to octamer related sequences from the enhancer of human papillomavirus type 18. The activity and intracellular distribution of p92 is regulated by extracellular signals. In serum starved Hela-fibroblast hybrid cells p92 is localized to the cytosol. Serum stimulation leads to nuclear import of p92. In fractions of asynchronously growing cells, which were separated according to cell cycle phases into G1, S, and G2 populations by centrifugal elutriation, p92 DNA binding is confined to S phase. In binding site blots however, p92 DNA binding activity is also present in G1 and G2. In G1 and G2 DNA binding activity of p92 is masked by a novel nuclear inhibitor I-92. The cyclic association of p92 with its inhibitor I-92 provides a new mechanism of regulating S phase dependent activity of a sequence specific DNA binding protein.Keywords
This publication has 41 references indexed in Scilit:
- Nuclear localization of c-Fos, but not v-Fos proteins, is controlled by extracellular signalsCell, 1990
- Casein kinase II enhances the DNA binding activity of serum response factor.Genes & Development, 1990
- The retinoblastoma susceptibility gene product undergoes cell cycle-dependent dephosphorylation and binding to and release from SV40 large TCell, 1990
- The product of the retinoblastoma susceptibility gene has properties of a cell cycle regulatory elementCell, 1989
- Induction of nuclear transport with a synthetic peptide homologous to the SV40 T antigen transport signalCell, 1986
- Platelet-derived growth factor induces rapid but transient expression of the c-fos gene and proteinNature, 1984
- Proteins shifting from the cytoplasm into the nuclei during early embryogenesis of Drosophila melanogasterDevelopmental Biology, 1984
- Nucleocytoplasmic distribution of snRNPs and stockpiled snRNA-binding proteins during oogenesis and early development in Xenopus laevisCell, 1983
- Inhibition of BALB/c‐3T3 cells in late G1: Commitment to DNA synthesis controlled by somatomedin CJournal of Cellular Physiology, 1981
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970