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The FK506-binding protein, Fpr4, is an acidic histone chaperone

By Haijie Xiao, Vaughn Jackson and Ming Lei

Abstract

AbstractFpr4, a FK506-binding protein (FKBP), is a recently identified novel histone chaperone. How it interacts with histones and facilitates their deposition onto DNA, however, are not understood. Here, we report a functional analysis that shows Fpr4 forms complexes with histones and facilitates nucleosome assembly like previously characterized acidic histone chaperones. We also show that the chaperone activity of Fpr4 resides solely in an acidic domain, while the peptidylprolyl isomerase domain conserved among all FKBPs inhibits the chaperone activity. These observations argue that Fpr4, while unique structurally, deposits histones onto DNA for nucleosome assembly through the well-established mechanism shared by other chaperones

Publisher: Published by Elsevier B.V.
Year: 2006
DOI identifier: 10.1016/j.febslet.2006.06.093
OAI identifier:

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