The FK506-binding protein, Fpr4, is an acidic histone chaperone. FEBS Lett 2006 Aug 07;580(18):4357-64
Date
07/19/2006Pubmed ID
16846601DOI
10.1016/j.febslet.2006.06.093Scopus ID
2-s2.0-33746344330 (requires institutional sign-in at Scopus site) 34 CitationsAbstract
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.
Author List
Xiao H, Jackson V, Lei MAuthor
Vaughn Jackson PhD Emeritus Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Histone ChaperonesHistones
Molecular Chaperones
Nucleosomes
Protein Structure, Tertiary
Saccharomyces cerevisiae Proteins
Tacrolimus Binding Proteins
