Not just for coding: a new role for histone tails in replication enzyme activation
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Updated: Mar 10, 2026

Examination of Proteins Bound to Nascent DNA in Mammalian Cells Using BrdU-ChIP-Slot-Western Technique
Published on: January 14, 2016
Anja-Katrin Bielinsky1, Wendy Leung1
1Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN, USA.
Abstract:
The processing of Okazaki fragments when they are assembled into nucleosomes has received little attention. In this issue of The FEBS Journal, Seo and colleagues show that binding to histone tails stimulates the enzymatic activity of flap endonuclease 1 (Rad27). Histone tails are structurally similar to the C terminus of Rad27 and can thus mimic its autostimulatory function. This study highlights an active regulatory role for nucleosomes on DNA metabolism.
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