Wei Yang, Ph.D.


LMB
STRUCTURE & MECHANISM OF DNA REPAIR, REPLICATION & RECOMBINATION
NIDDK, National Institutes of Health
Building 5 , Room B107
5 Memorial Dr.
Bethesda, MD 20814
Tel: 301-402-4645
Fax: 301-496-0201
Email: weiy@mail.nih.gov

Wei Yang, Ph.D.

Research Website:


Education / Previous Training and Experience:
B.A., SUNY at Stony Brook, 1985
M.A., Columbia University, 1986
Ph.D., Columbia University, 1991


Research Statement:

My group is interested in studying DNA recombination, repair and replication, in particular V(D)J recombination, methyl-directed mismatch repair and translesion DNA synthesis. We use X-ray crystallography, molecular biology and various biochemical and biophysical approaches to find out the molecular mechanisms in these biological processes.

We have more information posted on the Structural Biology Section home page.



Selected Publications:

Yang, W., Lee, J. Y. and Nowotny, M. Making and breaking nucleic acids: two-Mg2+-ion catalysis and substrate specificity Molecular Cell(22): 5-13, 2006.

Yang, W. Poor base stacking at DNA lesions may initiate recognition by many repair proteins DNA Repair(6): 654-66, 2006.

Nowotny, M. and Yang, W. Stepwise analyses of metal ions in RNase H catalysis: from substrate destabilization to product release EMBO J.(25): 1924-33, 2006.

Lee, J. Y. and Yang, W. UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke Cell (in press), 2006.

Guarné, A., Brendler T., Zhao, Q., Ghirlando, R., Austin, S., and Yang, W. Crystal structure of a SeqA-N filament: implications for DNA replication and chromosome organization EMBO J.(24): 1502-11, 2005.

Nowotny, M., Gaidamakov, S. A., Crouch, R. J., and Yang., W. Crystal structures of RNase H bound to an RNA: substrate specificity and metal-dependent catalysis Cell(121): 1005-16, 2005.

Vaisman A., Ling, H., Woodgate, R., and Yang, W. Fidelity of Dpo4: effect of metal ions, nucleotide selection and pyrophosphorolysis EMBO J.(24): 2957-67, 2005.

Lee, J. Y., Chang, J., Joseph, N. Ghirlando, R., Desirazu, N. R., and Yang, W. MutH complexed with hemi- and unmethylated DNAs: coupling base recognition and DNA cleavage Molecular Cell(20): 155-66, 2005.

Yang W. Portraits of a Y-family DNA polymerase FEBS Lett.(579): 868-72, 2005.

Ling, H, Sayer, J.M., Plosky, B.S., Yagi, H., Boudsocq, F., Woodgate, R., Jerina, D. M. and Yang, W. Crystal structure of a benzo[a]pyrene diol epoxide adduct in a ternary complex with a DNA polymerase PNAS(101): 2265-2269, 2004.

Ling, H, Boudsocq, F., Woodgate, R. and Yang, W. Snapshots of replication through an abasic lesion: structural basis for base substitution and frameshift Molecular Cell(13): 751-762, 2004.

Guarné, A., Ramon-Maiques, S., Wolff, E. M., Ghirlando, R., Hu, X., Miller, J. H., and Yang, W. Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair EMBO J.(23): 4134-45, 2004.

Alani, E., Lee, J. Y., Schofield, M. J., Kijas, A. W., Hsieh, P., and Yang, W. Crystal structure and biochemical analysis of the MutS-ADP·BeF3- complex suggests a conserved mechanism for ATP interactions in mismatch repair JBC(278): 16088-16094, 2003.

Junop, M. S., Yang, W., Funchain, P., Clendenin, W. and Miller, J. H. In vitro and in vivo studies of MutS, MutL and MutH mutants: correlation of mismatch repair and DNA recombination DNA Repair(2): 387-405, 2003.

Hu, X., Machius, M., and Yang. W. Monovalent cation dependence and pre- ference of GHKL ATPases and kinases FEBS Lett.(544): 268-273, 2003.

Ling, H, Boudsocq, F., Plosky, B., Woodgate, R. and Yang, W. Replication of a cis-syn thymine dimer at atomic resolution Nature(424): 1083-1087, 2003.

Guarné, A., Zhao, Q.-H. Ghirlando, R.. and Yang, W. SeqA complexed with hemimethylated DNA: negative modulation of E. coli replication initiation Nat. Struct. Biol.(9): 839-843, 2002.

Junop, M. S., Obmolova, G., Rausch, K., Hsieh, P and Yang, W. Composite active site of an ABC ATPsae: MutS uses ATP to verify mismatch recognition and authorize DNA repair Mol. Cell(7): 1-12, 2001.

Ling, H., Boudsocq, F., Woodgate, R. and Yang, W. Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass Cell(107): 91-102, 2001.

Guarné, A., Junop, M. S. and Yang, W. Structure and function of the N-terminal 40kDa fragment of human PMS2: a monomeric GHL ATPase EMBO J.(20): 5521-5531, 2001.

Junop, M. S., Modesti, M., Guarne, A., Gellert, M. and Yang, W. Crystal structure of the Xrcc4 DNA repair protein and implications for end joining EMBO J.(19): 5962-5970, 2000.

Obmolova, G., Ban, C., Hsieh, P and Yang, W. Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA Nature(407): 703-710, 2000.

Ban, C., Junop, M. S. and Yang, W Transformation of MutL by ATP Binding and hydrolysis: a switch in DNA mismatch repair Cell(97): 85-97, 1999.

Ban, C. and Yang, W. Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis Cell(95): 541-552, 1998.

Ban C Yang W Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases. EMBO J (17): 1526-34, 1998. [Full Text/Abstract]




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Page last updated: December 17, 2008

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