Jianhua Fu, PhD
Associate Professor
Locations
- Biochemistry
BSB 303
Contact Information
Biography
Dr. Fu received his PhD degree in Protein Crystallography from University of Pittsburgh in 1994. He spent a postdoctoral period in the laboratory of Roger Kornberg at Stanford University School of Medicine, where he cracked the phase problem in determining the crystallographic structure of RNA Polymerase II. Dr. Fu received fellowship awards from Universitywide AIDS Research Program (University of California) and American Cancer Society. Since 2000, his laboratory has been funded by the NIH to study the structural mechanism of RNA polymerase II machinery. Dr. Fu joined the faculty at Medical College of Wisconsin in 2007. Dr. Fu welcomes MCW graduate students to discuss prospects of thesis research in the area of Structural Biology. Potential postdoctoral scientists are encouraged to communicate their interests as well.
Education
PhD, University of Pittsburgh, 1994
Research Interests
Structure of the 12-subunit RNA polymerase II refined with the aid of anomalous diffraction data.
This figure shows the most complete structure of RNA Polymerase II (Pol II), the enzyme that reads genetic sequences from chromosomes in the nucleus of a cell. The Pol II model is rendered in the form of ribbons (most of it in blue) and laid over a background image of chromosomal DNA. The structural work was performed in the Fu lab by utilizing the power of anomalous scattering from 8 Zn2+ ions bound intrinsically in the polymerase. This latest model reveals the previously undetermined loop (green) that is implicated in contacting the general transcription factor TFIIF, and defines conformation for the loop (orange) that crosslinks with TFIIE. 
Several functionally significant elements are highlighted as follows: yellow, Fork Loop-1; grey-brown, Fork Loop-2; pink, Rudder and red (sphere), the catalytic Mg2+ site. The chromosomal DNA is depicted for its unraveling at the different levels, from the sister chromatids to 30-nm chromatin fiber and 10-nm nucleosomal array.
This work is described in: Meyer PA, Ye P, Suh MH, Zhang M, Fu J., J Biol Chem. 2009 Mar 16. [Epub ahead of print]
Publications
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Structures and Functions of the Multiple KOW Domains of Transcription Elongation Factor Spt5.
(Meyer PA, Li S, Zhang M, Yamada K, Takagi Y, Hartzog GA, Fu J.) Mol Cell Biol. 2015 Oct;35(19):3354-69.
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Ccr4-Not and TFIIS Function Cooperatively To Rescue Arrested RNA Polymerase II.
(Dutta A, Babbarwal V, Fu J, Brunke-Reese D, Libert DM, Willis J, Reese JC.) Mol Cell Biol. 2015 Jun 01;35(11):1915-25.
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(Babbarwal V, Fu J, Reese JC.) J Biol Chem. 2014 Nov 28;289(48):33125-30.
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The Spt4-Spt5 complex: a multi-faceted regulator of transcription elongation.
(Hartzog GA, Fu J.) Biochim Biophys Acta. 2013 Jan;1829(1):105-15.
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Mutual remodeling and conformation grid: a mediator code?
(Meyer PA, Fu J.) Structure. 2012 May 09;20(5):755-7.
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The multifunctional Ccr4-Not complex directly promotes transcription elongation.
(Kruk JA, Dutta A, Fu J, Gilmour DS, Reese JC.) Genes Dev. 2011 Mar 15;25(6):581-93.
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A dual interface determines the recognition of RNA polymerase II by RNA capping enzyme.
(Suh MH, Meyer PA, Gu M, Ye P, Zhang M, Kaplan CD, Lima CD, Fu J.) J Biol Chem. 2010 Oct 29;285(44):34027-38.
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(Chang WH, Chiu MT, Chen CY, Yen CF, Lin YC, Weng YP, Chang JC, Wu YM, Cheng H, Fu J, Tu IP.) Structure. 2010 Jan 13;18(1):17-27.
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Structure of the 12-subunit RNA polymerase II refined with the aid of anomalous diffraction data.
(Meyer PA, Ye P, Suh MH, Zhang M, Fu J.) J Biol Chem. 2009 May 08;284(19):12933-9.
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Phasing RNA polymerase II using intrinsically bound Zn atoms: an updated structural model.
(Meyer PA, Ye P, Zhang M, Suh MH, Fu J.) Structure. 2006 Jun;14(6):973-82.
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(Suh MH, Ye P, Zhang M, Hausmann S, Shuman S, Gnatt AL, Fu J.) Proc Natl Acad Sci U S A. 2005 Nov 29;102(48):17314-9.
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(Zhang Z, Fu J, Gilmour DS.) Genes Dev. 2005 Jul 01;19(13):1572-80.