Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 13, Issue 10, Pages 921-929Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1147
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Funding
- NIA NIH HHS [P01 AG031862-010001, P01 AG031862] Funding Source: Medline
- NIGMS NIH HHS [Y01 GM000080, R01 GM060293, Y1 GM-0080-3, R01 GM060293-01] Funding Source: Medline
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Human HIRA, ASF1a, ASF1b and CAF-1 are evolutionally conserved histone chaperones that form multiple functionally distinct chromatin-assembly complexes, with roles linked to diverse nuclear process, such as DNA replication and formation of heterochromatin in senescent cells. We report the crystal structure of an ASF1a-HIRA heterodimer and a biochemical dissection of ASF1a's mutually exclusive interactions with HIRA and the p60 subunit of CAF-1. The HIRA B domain forms an antiparallel beta-hairpin that binds perpendicular to the strands of the beta-sandwich of ASF1a, via beta-sheet, salt bridge and van der Waals contacts. The N- and C-terminal regions of ASF1a and ASF1b determine the different affinities of these two proteins for HIRA, by contacting regions outside the HIRA B domain. CAF-1 p60 also uses B domain -like motifs for binding to ASF1a, thereby competing with HIRA. Together, these studies begin to define the molecular determinants of assembly of functionally diverse macromolecular histone chaperone complexes.
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