Histone H2A.Z acid patch residues required for deposition and function |
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Authors: | Kurt Jensen Maria Soledad Santisteban Craig Urekar M Mitchell Smith |
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Institution: | (1) Department of Microbiology, University of Virginia Health System, University of Virginia, P.O. Box 800734, Charlottesville, VA 22908-0734, USA;(2) Present address: Department of Neurology, McKnight Brain Institute, University of Florida, 100 S. Newell Dr., P.O. Box 100236, Gainesville, FL 32610-0236, USA;(3) Present address: Department of Biology, University of North Carolina at Pembroke, One University Drive, P.O. Box 1510, Pembroke, NC 28372-1510, USA |
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Abstract: | The incorporation of histone variants is one mechanism used by the eukaryotic cell to alter the generally repressive chromatin
template. However, the exact molecular mechanisms that direct this incorporation are not well understood. The SWR1 chromatin
remodeling complex that binds to and directs incorporation of histone variant H2A.Z into chromatin has been characterized,
but significantly less information is available concerning the requirements on the H2A.Z target molecule. We performed an
unbiased mutagenic screen designed to elucidate the function of H2A.Z in Saccharomyces cerevisiae. The screen identified residues within the conserved acidic patch of H2A.Z as being important for the function of the variant.
We characterized single point mutations in the patch that are phenotypically sensitive to a variety of growth conditions and
are expressed at lower protein levels, but are functionally defective (htz1-D99A, htz1-D99K, and htz1-E101K). The mutants were significantly less detectable by chromatin immunoprecipitation at PHO5, a gene previously described to be enriched for H2A.Z. These results identify acidic patch residues of H2A.Z that are critical
for mediating deposition and function in chromatin, and represent potential candidates for the interaction of H2A.Z with its
deposition and/or targeting machinery. |
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