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Cell Cycle-Regulated Binding of Nuclear Proteins to Elements within a Mouse H3.2 Histone Gene

Nikola K. Kaludov, Tammy L. Bowman, Eric M. Sikorski and Myra M. Hurt
Proceedings of the National Academy of Sciences of the United States of America
Vol. 93, No. 9 (Apr. 30, 1996), pp. 4465-4470
Stable URL: http://www.jstor.org/stable/39269
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Cell Cycle-Regulated Binding of Nuclear Proteins to Elements within a Mouse H3.2 Histone Gene
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Abstract

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, α and Ω , 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.

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