Journal
FEBS LETTERS
Volume 580, Issue 18, Pages 4357-4364Publisher
WILEY
DOI: 10.1016/j.febslet.2006.06.093
Keywords
histone chaperone; nucleosome assembly; FKBP
Funding
- NIGMS NIH HHS [GM6264901] Funding Source: Medline
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Fpr4, 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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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