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[Results] Wang Zhanxin a research group of Beijing Normal University's College of Life Sciences published an academic paper on PNAS to reveal eukaryotic transcription elongation factor Paf1 complex

Published: 2018-09-28

[Results] Wang Zhanxin, a research group of Beijing Normal University's College of Life Sciences, published an academic paper on PNAS to reveal the crystal structure and molecular assembly mechanism of the core component of eukaryotic transcription elongation factor Paf1 complex



Article source: College of Life Sciences



On September 17, 2018, the international authoritative academic journal "PNA" online published the paper of Professor Wang Zhanxin, who is from the key laboratory of the Ministry of Education of Cellular Proliferation and Regulatory Biology, School of Life Sciences, Beijing Normal University, entitled "Transcriptional elongation factor Paf1 core complex adopts a spirally wrapped solenoidal topology". The article of elongation factor Paf1 core complex adopts a spirally wrapped solenoidal topology reports the crystal structure of 2.9 angstrom resolution of the core ternary component Ctr9-Paf1-Cdc73 of the transcription elongation factor Paf1 complex in thermophilic yeast. The Paf1 complex is a transcriptional elongation factor of RNA polymerase II specific to eukaryotes. It is involved in the transcriptional regulation of transcription initiation, elongation to termination, and is closely related to various histone modifications, regulating transcription by epigenetic means. Mutation or abnormal expression of multiple components in the Paf1 complex is associated with human cancer. After more than five years of unremitting efforts, Wang Zhanxin's research team analyzed the crystal structure of the Ctr9-Paf1-Cdc73 ternary complex in the core of the Paf1 complex. This work reveals the fine structure and assembly method of the core region of the Paf1 complex for the first time. The mechanism by which the Paf1 complex is involved in transcriptional regulation and epigenetic regulation provides a molecular basis for structural analysis to explain the relationship between the mutation of the Paf1 complex (such as the mutation of CTR9) and cancer, and provide targets for the targeted therapy to the disease caused by the abnormality of the complex.



Figure 1: Schematic diagram of the core structure of Ctr9-Paf1-Cdc73 ternary composite and the structure of some components



Wang Zhanxin's doctoral students Deng Puzhen and Zhou Yuqiao are the co-first authors of this article. Professor Wang Zhanxin and Professor Dinshaw Patel of the Sloan Kettering Cancer Institute of the United States are co-authors of this article. The Cell Proliferation and Regulatory Biology of Beijing Normal University, Key laboratory of the Ministry of Education is the first completion unit. Professor Robert Roeder of Rockefeller University and Professor Jaehoon Kim of KAIST University in South Korea provided valuable advice for the completion of the work. The work was funded by the National Natural Science Foundation of China, the Independent Research Fund of Beijing Normal University, and the “Thousands of Young People” Foundation. The Shanghai Synchrotron Radiation Source (SSRF) provided important technical support for the research.


The original link:

http://www.pnas.org/content/early/2018/09/11/1812256115



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