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Reference: Liu Y, et al. (2010) Structural analysis of Rtt106p reveals a DNA binding role required for heterochromatin silencing. J Biol Chem 285(6):4251-62

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Abstract


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 A 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 as well as a novel double-stranded DNA-binding region has 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.

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Journal Article
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Liu Y, Huang H, Zhou BO, Wang SS, Hu Y, Li X, Liu J, Zang J, Niu L, Wu J, ... Show all
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