PhD, Northwestern University
Office Phone: 847.491.8526
The He lab is interested in understanding the molecular mechanisms by which large, multi-subunit complexes engage in DNA-centric processes using cryo-electron microscopy (cryo-EM) and other biophysical and biochemical approaches. We focus on two main topics: (1) how eukaryotic gene transcription is regulated at different stages, and (2) how various types of DNA damage are repaired and why deficiencies in these repair pathways lead to pathology of cancer predisposition or accelerated aging.
Cryo-EM is a powerful tool well suited for revealing macromolecular assemblies’ structures at moderately high to near atomic resolution. It requires considerably smaller amount of sample, is not limited by the size of the system of interest, and is well equipped for sorting conformational/biochemical heterogeneity in a single sample under close to physiological conditions. These advantages, together with ongoing technical breakthroughs (direct electron detector and phase plate), make cryo-EM a unique tool to further our structural understanding of complicated cellular processes.
Structural basis of transcription promoter opening using single particle cryo-EM. He Y, Yan C, Inouye C, Fang J, Tjian R, Ivanov I, and Nogales E. 2015 Manuscript in preparation
Structural visualization of key steps in human transcription initiation. He Y, Fang J, Taatjes DJ, and Nogales E. 2013 Nature 495, 481-6.
Structure of the 30 kDa Sin3-Associated Protein (SAP30) in Complex with the Mammalian Sin3A Corepressor and its Role in Nucleic Acid Binding. Xie T, He Y, Korkeamaki H, Zhang Y, Imhoff R, Lohi O, Radhakrishnan I. 2011 J. Biol. Chem. 286, 27814–24.
Solution structure of a novel zinc finger motif in the SAP30 polypeptide of the Sin3 corepressor complex and its potential role in nucleic acid recognition. He Y, Imhoff R, Sahu A, and Radhakishnan I. 2009 Nucleic Acids Res. 37, 2142–2152.
Solution NMR studies of apo-mSin3A and mSin3B reveal that the PAH1 and PAH2 domains are structurally independent. He Y, and Radhakishnan I. 2008 Protein Sci. 17, 171-175.
Structural basis for ubiquitin recognition by SH3 domains. He Y, Hicke L, and Radhakishnan I. 2007 J. Mol. Biol. 373, 190-196.
Ubiquitin binds to and regulates a subset of SH3 domains. Stamenova SD, French ME, He Y, Francis SA, Kramer ZB, and Hicke L. 2007 Mol. Cell 25, 273-284.