Article abstract
Nature Structural & Molecular Biology 14, 779 - 784 (2007)
Published online: 15 July 2007 | doi:10.1038/nsmb1269
The multifunctional human p100 protein 'hooks' methylated ligands
Neil Shaw1,6, Min Zhao2,6, Chongyun Cheng1, Hao Xu2, Juha Saarikettu3, Yang Li1, Yurong Da4, Zhi Yao4, Olli Silvennoinen3, Jie Yang4, Zhi-Jie Liu1, Bi-Cheng Wang2 & Zihe Rao1,5
Abstract
The human p100 protein is a vital transcription regulator that increases gene transcription by forming a physical bridge between promoter-specific activators and the basal transcription machinery. Here we demonstrate that the tudor and SN (TSN) domain of p100 interacts with U small nuclear ribonucleoprotein (snRNP) complexes, suggesting a role for p100 in the processing of precursor messenger RNA. We determined the crystal structure of the p100 TSN domain to delineate the molecular basis of p100's proposed functions. The interdigitated structure resembles a hook, with a hinge controlling the movement and orientation of the hook. Our studies suggest that a conserved aromatic cage hooks methyl groups of snRNPs and anchors p100 to the spliceosome. These structural insights partly explain the distinct roles of p100 in transcription and splicing.
- National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
- Southeast Collaboratory for Structural Genomics, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, USA.
- Institute of Medical Technology, University of Tampere and Tampere University Hospital, FIN-33014 Tampere, Finland.
- Department of Immunology, Tianjin Medical University, Tianjin, 300070, China.
- Laboratory of Structural Biology, Life Science Building, Tsinghua University, Beijing 100084, China.
- These authors contributed equally to this work.
Correspondence to: Zhi-Jie Liu1 e-mail: zjliu@ibp.ac.cn
Correspondence to: Jie Yang4 e-mail: yangj@tijmu.edu.cn
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