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Article

Structural analysis of Rtt106p reveals a DNA binding role required for heterochromatin silencing.

The Journal of biological chemistry - 5 Feb 2010

Liu Yiwei, Huang Hongda, Zhou Bo O, Wang Shan-Shan, Hu Yingxia, Li Xu, Liu Jianping, Zang Jianye, Niu Liwen, Wu Jihui, Zhou Jin-Qiu, Teng Maikun, Shi Yunyu

Abstract excerpt

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...

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Share to Crystallography, X-Ray
Share to DNA, Fungal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Silent Information Regulator Proteins, Saccharomyces cerevisiae

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Identifiers

PMID: 20007951
DOI: 10.1074/jbc.M109.055996
PMCID: PMC2824209

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