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Structural studies of the histone chaperone Hif1, a component of the Hat1 chromatin assembly complex
Author(s) -
Bigeh Allison,
Pickle Elyssa,
Bagley Michael J.,
Seangmany Nessa,
Dutnall Robert N.
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.925.2
Subject(s) - histone h1 , histone code , sap30 , biology , histone , histone acetyltransferase , chromatin , histone h2a , histone h4 , histone octamer , biochemistry , histone methyltransferase , microbiology and biotechnology , dna , nucleosome
The Hat1 chromatin assembly complex contains the Hat1 histone acetyltransferase and two Hat1‐interacting factors: Hat2 and Hif1. The Hat1 enzyme specifically acetylates histone H4 while Hat2 and Hif1 are both histone binding proteins. These three proteins form cytoplasmic and nuclear complexes that are part of a pathway that deposits newly synthesized histone H3 and histone H4 onto DNA. In yeast, Hat1 complexes contribute to gene regulation and DNA repair. Hat1, Hat2 and Hif1 are each highly conserved and form similar complexes in organisms ranging from yeast to humans. We are using biochemical and biophysical methods to study the structure and function of the Hif1 protein from yeast with the goal of understanding how it contributes to the activity of the Hat1 chromatin assembly complex. Hif1 has histone chaperone activity and contains four tetratricopeptide (TPR) sequence motifs. We have evidence that like its human counterpart, bacterially expressed yeast Hif1 is an oligomer forming dimers and possibly tetrameric assemblies. The bacterially expressed protein also interacts with histones. We are currently using truncation mutants to map the regions of the Hif1 protein involved in oligomer formation and histone binding. We are also using a variety of biochemical and biophysical methods to probe the strength and specificity of Hif1‐histone interactions.