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Think and Do The Extraordinary

Hong Wang

Associate Professor

Riddick Hall 258E


Hong Wang obtained her Ph. D. in physics from the University of North Carolina in 2003 specializing in materials and biophysics. She then took a postdoctoral training from 2004-2008 in DNA repair and single-molecule imaging, at the U. S. National Institute of Environmental Health Sciences. Following this, she then served from 2008-2011 in a postdoctoral training in telomere biology and single-molecule imaging at the University of Pittsburgh. She joined the department of Physics in the fall of 2011 bring with her a highly competitive NIH grant.

Research Description

Her research focuses on single-molecule experimental investigations of the structure-function relationships that govern the maintenance of telomeres. Telomeres are nucleoprotein structures that cap the ends of linear chromosomes. Dysfunctional telomeres are important contributing factors in aging and tumorigenesis. Telomeric DNA sequences show a higher susceptibility to certain DNA damaging agents than random DNA sequences. The goal of her current research is to use two highly innovative and complementary single-molecule imaging techniques (atomic force microscopy and fluorescence imaging) together with quantum dot labeled proteins to investigate the effects of DNA damage on the conformational and dynamic properties of telomeric DNA structure and telomere binding proteins. She work concentrates on dynamic protein-DNA interactions in real time and at the single-molecule level using techniques developed by her group to perform a unique DNA tight-rope assay. This assay has enabled visualization of DNA in its extended form several micrometers above the surface and to observe movements of individual proteins with up to 17 nm positional accuracy and 50 ms temporal resolution using oblique-angle fluorescence microscopy.


Complete list of publications

Selected Publications

Single-Molecule Study of TRF2 Mediated DNA Compaction using Physiologically Relevant Long Telomeric DNA.
P. Kaur, R. Barnes, H. Pan, P. Opresko, R. Riehn, H. Wang
Biophysical Journal, 116,, (2019), 505a.

Cohesin SA2 is a sequence-independent DNA-binding protein that recognizes DNA replication and repair intermediates
P. Countryman, Y. Fan, A. Gorthi, H. Pan, J. Strickland, P. Kaur, X. Wang, J. Lin, X. Lei, C. White, C. You, N. Wirth, I. Tessmer, J. Piehler, R. Riehn, A. Bishop, Y. Tao, H. Wang
Journal of Biological Chemistry, 293(3), (2018), 1054–1069.

CpG and methylation-dependent DNA binding and dynamics of the methylcytosine binding domain 2 protein at the single-molecule level
H. Pan, S. Bilinovich, P. Kaur, R. Riehn, H. Wang & D. Williams
Nucleic Acids Research, 45(15), (2017), 9164–9177

Enhanced electrostatic force microscopy reveals higher-order DNA looping mediated by the telomeric protein TRF2
Kaur, P., Wu, D., Lin, J. G., Countryman, P., Bradford, K. C., Erie, D. A., Riehn, R., Opresko, P. L., Wang, H.,
Scientific Reports, 6, (2016), pp.20513-20513.

Functional interplay between SA1 and TRF1 in telomeric DNA binding and DNA-DNA pairing
Lin, J. G., Countryman, P., Chen, H. J., Pan, H., Fan, Y. L., Jiang, Y. Y., Kaur, P., Miao, W., Gurgel, G., You, C. J., Piehler, J., Kad, N. M., Riehn, R., Opresko, P. L., Smith, S., Tao, Y. J., Wang, H.,
Nucleic Acids Research, 44 (13), (2016), pp.6363-6376.

Visualizing the Path of DNA through Proteins Using DREEM Imaging
Wu, D., Kaur, P., Li, Z.M., Bradford, K.C., Wang, H. and Erie, D.A.
Molecular Cell, 61, (2016), pp.315-323.

Telomeres are partly shielded from ultraviolet-induced damage and proficient for nucleotide excision repair of photoproducts
Parikh, D., Fouquerel, E., Murphy, C.T., Wang, H. and Opresko, P.L.
Nature communications, 6, (2015), 8214

TRF1 and TRF2 use different mechanisms to find telomeric DNA but share a novel mechanism to search for protein partners at telomeres
Lin, J., Countryman, P., Buncher, N., Kaur, P., E, L., Zhang, Y., Gibson, G., You, C., Watkins, S.C., Piehler, Opesko, L. P., Kad, N., Wang, H.,
Nucleic Acids Research, 42 (4), (2014), 2493-2504

DNA polymerase δ stalls on telomeric lagging strand templates independently from G-quadruplex formation
Lormand, J.D., Buncher, N., Murphy, C.T., Kaur, P., Lee, M.Y., Burgers, P., Wang, H., Kunkel, T.A. and Opresko, P.L.,
Nucleic Acids Research, 41 (22), (2013), 10323-10333

Damaged DNA induced UV-damaged DNA-binding protein (UV-DDB) dimerization and its roles in chromatinized DNA repair
Yeh, J.I., Levine, A.S., Du, S., Chinte, U., Ghodke, H., Wang, H., Shi, H., Hsieh, C.L., Conway, J.F., Van Houten, B. et al.,
PNAS, 109(41), (2012), E2737-E2746

FIONA-AFM hybrid imaging with nm accuracy
Fronczek, D, Quammen, C., Wang, H., Kisker, C., Superfine R., Taylor, R., Erie, D.A., Tessmer, I,
Ultramicroscopy, 111(5), (2011), 350-5

Single molecule studies of physiologicaly relevant telomeric tails reveals POT1 mechanism for promoting G-quadruplex unfolding
Wang, H., Nora, G.J., Ghodke H., Opresko P.L.,
J Biol Chem., 286(9), (2011), 7479-89.

Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single-molecule fluorescence imaging of quantum dot labeled proteins
Kad, N., Wang, H., Kennedy, G.G., Warshaw, D.M., Van Houten, B.
Molecular Cell, 37(5), (2010), 702-13

Replication protein A stimulates the werner syndrome protein branch migration activity
Sowd, G., Wang, H., Pretto, D., Chazin, W.J., Opresko, P.L.
J Biol Chem., 11;284(50), (2009), 34682-91

The Werner syndrome helicase/exonuclease processes mobile D-loops through branch migration and degradation
Opresko, P.L., Sowd, G., and Wang, H.
PLoS ONE 4, e4825, (2009), PMC2653227

Efficient processing of TFO-directed psoralen DNA interstrand crosslinks by the UvrABC nuclease
Christensen, L.A., Wang, H., Van Houten, B., and Vasquez, K.M.
Nucleic Acids Res, 36, (2008), 7136-7145.

Functional characterization and atomic force microscopy of a DNA repair protein conjugated to a quantum dot
Wang, H., Tessmer, I., Croteau, D.L., Erie, D.A., and Van Houten, B.
Nano Lett., 8, (2008), 1631-1637.

UvrB domain 4, an autoinhibitory gate for regulation of DNA binding and ATPase activity
Wang, H., DellaVecchia, M.J., Skorvaga, M., Croteau, D.L., Erie, D.A. and Van Houten, B.
J Biol Chem, 281, (2006), 15227-15237.