The FK506-binding protein, Fpr4, is an acidic histone chaperone.
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.
Xiao
Haijie
H
Department of Microbiology and Molecular Genetics, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, 53226, USA.
Jackson
Vaughn
V
Lei
Ming
M
D056488:Histone Chaperones; D006657:Histones / Q000378:metabolism*; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D009707:Nucleosomes / Q000378:metabolism; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D022021:Tacrolimus Binding Proteins / Q000737:chemistry / Q000378:metabolism*
D056488:Histone Chaperones; D006657:Histones; D018832:Molecular Chaperones; D009707:Nucleosomes; D029701:Saccharomyces cerevisiae Proteins; D022021:Tacrolimus Binding Proteins; C513494:Fpr4 protein, S cerevisiae