Structural Analysis of Rtt106p Reveals a DNA Binding Role Required for Heterochromatin Silencing
Rtt106p is a Saccharomyces cerevisiae histone chaperone with roles in heterochromatin silencing and nucleosome assembly. The molecular mechanism by which Rtt106p engages in chromatin dynamics remains unclear. Here, we report the 2.5 {angstrom} crystal structure of the core domain of Rtt106p, which adopts an unusual 'double pleckstrin homology' domain architecture that represents a novel structural mode for histone chaperones. A histone H3-H4-binding region and a novel double-stranded DNA-binding region have been identified. Mutagenesis studies reveal that the histone and DNA binding activities of Rtt106p are involved in Sir protein-mediated heterochromatin formation. Our results uncover the structural basis of the diverse functions of Rtt106p and provide new insights into its cellular roles.
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
- Sponsoring Organization:
- DOE - OFFICE OF SCIENCE
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 1019668
- Report Number(s):
- BNL-95514-2011-JA; JBCHA3; TRN: US201115%%308
- Journal Information:
- Journal of Biological Chemistry, Vol. 285, Issue 6; ISSN 0021-9258
- Country of Publication:
- United States
- Language:
- English
Similar Records
The Cac2 subunit is essential for productive histone binding and nucleosome assembly in CAF-1
Structure of the human histone chaperone FACT Spt16 N-terminal domain