Weidong Wang, Ph.D.
Laboratory of Genetics
251 Bayview Boulevard
Baltimore, MD 21224
The establishment and maintenance of transcriptionally active and inactive chromatin structure in higher eucaryotes is key for global gene regulation during development, differentiation and adaptation to environmental stimuli. Evidence accumulated during the last two decades indicates that chromatin structures are remodeled when multipotent precursor cells develop into terminally-differentiated cells. However, the underlying mechanism of chromatin remodeling is poorly understood, primarily because molecules that remodel chromatin structures have been discovered only recently. These complexes can be classified into two different families: one, the histone acetyltransferase or deacetylase complexes which alter the chromatin structure by covalently modifying the tails of histones; the other, the ATP-Dependent Chromatin-Remodeling (ADCR) complexes which use the energy of ATP to disrupt non-covalent DNA-histone contacts. The main focus of our lab is to purify and characterize mammalian ADCR complexes.
Dr. Wang was trained as a biochemist and a molecular biologist at both UCLA, where he obtained his Ph.D., and Stanford University, where he worked as a postdoctoral fellow. His research has focused on the regulation of mammalian gene expression at the chromatin level. He has purified to homogeneity one of the first ATP-dependent chromatin-remodeling complexes in mammals, and has subsequently cloned all the subunits within one complex. His current projects include characterization of novel chromatin-remodeling complexes involved in human ATRX syndrome (X-linked mental retardation and a-thalassemia); helicase complexes involved in the Werner premature aging syndrome, Bloom syndrome, and Rothmund-Thompson syndrome; and a ubiquitin ligase complex involved in a genomic instability disease, Fanconi anemia.
Yan Z, Guo R, Paramasivam M, Shen W, Ling C, Fox D 3rd, Wang Y, Oostra AB, Kuehl J, Lee DY, Takata M, Hoatlin ME, Schindler D, Joenje H, de Winter JP, Li L, Seidman MM, Wang W. A ubiquitin-binding protein, FAAP20, links RNF8-mediated ubiquitination to the Fanconi anemia DNA repair network. Mol Cell. 2012;47(1):61-75.
Xu D, Muniandy P, Leo E, Yin J, Thangavel S, Shen X, Ii M, Agama K, Guo R, Fox D 3rd, Meetei AR, Wilson L, Nguyen H, Weng NP, Brill SJ, Li L, Vindigni A, Pommier Y, Seidman M, Wang W. Rif1 provides a new DNA-binding interface for the Bloom syndrome complex to maintain normal replication. EMBO J. 2010;29(18):3140-55.
Ahmad M, Xue Y, Lee SK, Martindale JL, Shen W, Li W, Zou S, Ciaramella M, Debat H, Nadal M, Leng F, Zhang H, Wang Q, Siaw GE, Niu H, Pommier Y, Gorospe M, Hsieh TS, Tse-Dinh YC, Xu D, Wang W. RNA topoisomerase is prevalent in all domains of life and associates with polyribosomes in animals. Nucleic Acids Res. 2016;44(13):6335-49.
Xu D, Shen W, Guo R, Xue Y, Peng W, Sima J, Yang J, Sharov A, Srikantan S, Yang J, Fox D 3rd, Qian Y, Martindale JL, Piao Y, Machamer J, Joshi SR, Mohanty S, Shaw AC, Lloyd TE, Brown GW, Ko MS, Gorospe M, Zou S, Wang W. Top3β is an RNA topoisomerase that works with fragile X syndrome protein to promote synapse formation. Nat Neurosci. 2013;16(9):1238-47.
Meetei AR, Medhurst AL, Ling C, Xue Y, Singh TR, Bier P, Steltenpool J, Stone S, Dokal I, Mathew CG, Hoatlin M, Joenje H, de Winter JP, Wang W. A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M. Nat Genet. 2005;37(9):958-63.
Related Scientific Focus Areas
Molecular Biology and Biochemistry
Genetics and Genomics
This page was last updated on September 5th, 2017