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Structure of a CENP-A -- histone H4 heterodimer in complex with chaperone HJURP.
- Source :
-
Genes & Development . 5/1/2011, Vol. 25 Issue 9, p4-4. 1p. - Publication Year :
- 2011
-
Abstract
- In higher eukaryotes, the centromere is epigenetically specified by the histone H3 variant Centromere Protein-A (CENP-A). Deposition of CENP-A to the centromere requires histone chaperone HJURP (Holliday junction recognition protein). The crystal structure of an HJURP-CENP-A-histone H4 complex shows that HJURP binds a CENP-A-H4 heterodimer. The C-terminal β-sheet domain of HJURP caps the DNA-binding region of the histone heterodimer, preventing it from spontaneous association with DNA. Our analysis also revealed a novel site in CENP-A that distinguishes it from histone H3 in its ability to bind HJURP. These findings provide key information for specific recognition of CENP-A and mechanistic insights into the process of centromeric chromatin assembly. [ABSTRACT FROM AUTHOR]
- Subjects :
- *HISTONES
*MOLECULAR chaperones
*PROTEINS
*CENTROMERE
*CHROMOSOMES
Subjects
Details
- Language :
- English
- ISSN :
- 08909369
- Volume :
- 25
- Issue :
- 9
- Database :
- Academic Search Index
- Journal :
- Genes & Development
- Publication Type :
- Academic Journal
- Accession number :
- 60995493
- Full Text :
- https://doi.org/10.1101/gad.2045111