Dr. Yang is the co-recipient of the 2011 Dorothy Crowfoot Hodgkin Award granted in recognition of exceptional contributions in protein science which profoundly influence our understanding of biology.
Surviving the Sun: Repair and bypass of DNA UV lesions†
Article first published online: 18 OCT 2011
Copyright © 2011 The Protein Society
Volume 20, Issue 11, pages 1781–1789, November 2011
How to Cite
Yang, W. (2011), Surviving the Sun: Repair and bypass of DNA UV lesions. Protein Science, 20: 1781–1789. doi: 10.1002/pro.723
- Issue published online: 18 OCT 2011
- Article first published online: 18 OCT 2011
- Accepted manuscript online: 24 AUG 2011 12:58PM EST
- Manuscript Accepted: 17 AUG 2011
- Manuscript Revised: 16 AUG 2011
- Manuscript Received: 29 JUL 2011
- 6-4 PP;
Structural studies of UV-induced lesions and their complexes with repair proteins reveal an intrinsic flexibility of DNA at lesion sites. Reduced DNA rigidity stems primarily from the loss of base stacking, which may manifest as bending, unwinding, base unstacking, or flipping out. The intrinsic flexibility at UV lesions allows efficient initial lesion recognition within a pool of millions to billions of normal DNA base pairs. To bypass the damaged site by translesion synthesis, the specialized DNA polymerase η acts like a molecular “splint” and reinforces B-form DNA by numerous protein–phosphate interactions. Photolyases and glycosylases that specifically repair UV lesions interact directly with UV lesions in bent DNA via surface complementation. UvrA and UvrB, which recognize a variety of lesions in the bacterial nucleotide excision repair pathway, appear to exploit hysteresis exhibited by DNA lesions and conduct an ATP-dependent stress test to distort and separate DNA strands. Similar stress tests are likely conducted in eukaryotic nucleotide excision repair.