| Title | ASF1 binds to a heterodimer of histones H3 and H4: a two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA. |
| Publication Type | Journal Article |
| Year of Publication | 2005 |
| Authors | English CM, Maluf NK, Tripet B, Churchill MEA, Tyler JK |
| Journal | Biochemistry |
| Volume | 44 |
| Issue | 42 |
| Pagination | 13673-82 |
| Date Published | 2005 Oct 25 |
| ISSN | 0006-2960 |
| Keywords | Cell Cycle Proteins, Chromatography, Gel, Chromatography, High Pressure Liquid, Dimerization, DNA, Histones, Molecular Chaperones, Molecular Weight, Nucleosomes, Saccharomyces cerevisiae Proteins, Ultracentrifugation |
| Abstract | The first step in the formation of the nucleosome is commonly assumed to be the deposition of a histone H3-H4 heterotetramer onto DNA. Antisilencing function 1 (ASF1) is a major histone H3-H4 chaperone that deposits histones H3 and H4 onto DNA. With a goal of understanding the mechanism of deposition of histones H3 and H4 onto DNA, we have determined the stoichiometry of the Asf1-H3-H4 complex. We have established that a single molecule of Asf1 binds to an H3-H4 heterodimer using gel filtration, amino acid, reversed-phase chromatography, and analytical ultracentrifugation analyses. We demonstrate that Asf1 blocks formation of the H3-H4 heterotetramer by a mechanism that likely involves occlusion of the H3-H3 dimerization interface. |
| DOI | 10.1021/bi051333h |
| Alternate Journal | Biochemistry |
| PubMed ID | 16229457 |
| PubMed Central ID | PMC4445473 |
| Grant List | R01 GM064475 / GM / NIGMS NIH HHS / United States R01 GM079154 / GM / NIGMS NIH HHS / United States R01 GM079154-01A1 / GM / NIGMS NIH HHS / United States GM64475 / GM / NIGMS NIH HHS / United States |
Related Faculty:
Jessica K. Tyler, Ph.D.