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Science 20 December 1991: Vol. 254. no. 5039, pp. 1814 - 1816 DOI: 10.1126/science.1684878
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Articles
Science, Vol 254, Issue 5039, 1814-1816
Copyright © 1991 by American Association for the Advancement of Science
Mitotic phosphorylation of the Oct-1 homeodomain and regulation of Oct-1 DNA binding activity
N Segil,
SB Roberts,
and
N Heintz
Laboratory of Molecular Biology, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021.
Oct-1 is a transcription factor involved in the cell cycle regulation of histone H2B gene transcription and in the transcription of other cellular housekeeping genes. Oct-1 is hyperphosphorylated as cells enter mitosis, and mitosis-specific phosphorylation is reversed as cells exit mitosis. A mitosis-specific phosphorylation site in the homeodomain of Oct-1 was phosphorylated in vitro by protein kinase A. Phosphorylation of this site correlated with inhibition of Oct-1 DNA binding activity in vivo and in vitro. The inhibition of Oct-1 DNA binding during mitosis suggests a mechanism by which the general inhibition of transcription during mitosis might occur.
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