3gyp

Publication Abstract from PubMed

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 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.

Structural analysis of Rtt106p reveals a DNA binding role required for heterochromatin silencing.,Liu Y, Huang H, Zhou BO, Wang SS, Hu Y, Li X, Liu J, Zang J, Niu L, Wu J, Zhou JQ, Teng M, Shi Y J Biol Chem. 2010 Feb 5;285(6):4251-62. Epub 2009 Dec 10. PMID:20007951^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.