Open AccessCell cycle-regulated binding of nuclear proteins to elements within a mouse H3.2 histone gene.
Author(s) -
Nikola Kaludov,
Tammy Bowman,
Eric M. Sikorski,
Myra M. Hurt
Publication year - 1996
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.93.9.4465
Subject(s) - biology , histone h2a , histone , microbiology and biotechnology , sap30 , chinese hamster ovary cell , origin recognition complex , nuclear protein , histone methyltransferase , histone code , histone h3 , dna replication , histone h1 , gene , genetics , eukaryotic dna replication , nucleosome , cell culture , transcription factor
The histone gene family in mammals consists of 15-20 genes for each class of nucleosomal histone protein. These genes are classified as either replication-dependent or -independent in regard to their expression in the cell cycle. The expression of the replication-dependent histone genes increases dramatically as the cell prepares to enter S phase. Using mouse histone genes, we previously identified a coding region activating sequence (CRAS) involved in the upregulation of at least two (H2a and H3) and possibly all nucleosomal replication-dependent histone genes. Mutation of two seven-nucleotide elements, alpha and omega, within the H3 CRAS causes a decrease in expression in stably transfected Chinese hamster ovary cells comparable with the effect seen upon deletion of the entire CRAS. Further, nuclear proteins interact in a highly specific manner with nucleotides within these sequences. Mutation of these elements abolishes DNA/protein interactions in vitro. Here we report that the interactions of nuclear factors with these elements are differentially regulated in the cell cycle and that protein interactions with these elements are dependent on the phosphorylation/dephosphorylation state of the nuclear factors.