dc.contributor.author | Blainey, Paul C. | |
dc.contributor.author | Oijen, Antoine van | |
dc.contributor.author | Banerjee, Anirban | |
dc.contributor.author | Verdine, Gregory L. | |
dc.contributor.author | Xie, X. Sunney | |
dc.date.accessioned | 2019-10-09T13:57:06Z | |
dc.date.issued | 2006 | |
dc.identifier.citation | Blainey, P. C., A. M. van Oijen, A. Banerjee, G. L. Verdine, and X. S. Xie. 2006. “A Base-Excision DNA-Repair Protein Finds Intrahelical Lesion Bases by Fast Sliding in Contact with DNA.” Proceedings of the National Academy of Sciences103 (15): 5752–57. https://doi.org/10.1073/pnas.0509723103. | |
dc.identifier.issn | 0027-8424 | |
dc.identifier.issn | 0744-2831 | |
dc.identifier.issn | 1091-6490 | |
dc.identifier.uri | http://nrs.harvard.edu/urn-3:HUL.InstRepos:41511305 | * |
dc.description.abstract | A central mystery in the function of site-specific DNA-binding proteins is the detailed mechanism for rapid location and binding of target sites in DNA. Human oxoguanine DNA glycosylase 1 (hOgg1), for example, must search out rare 8-oxoguanine lesions to prevent transversion mutations arising from oxidative stress. Here we report high-speed imaging of single hOgg1 enzyme molecules diffusing along DNA stretched by shear flow. Salt-concentration-dependent measurements reveal that such diffusion occurs as hOgg1 slides in persistent contact with DNA. At near-physiologic pH and salt concentration, hOgg1 has a subsecond DNA-binding time and slides with a diffusion constant as high as 5 x 10(6) bp(2)/S. Such a value approaches the theoretical upper limit for one-dimensional diffusion and indicates an activation barrier for sliding of only 0.5 kcal/mol (1 kcal = 4.2 W). This nearly barrierless Brownian sliding indicates that DNA glycosylases locate lesion bases by a massively redundant search in which the enzyme selectively binds 8-oxoguanine under kinetic control. | |
dc.language.iso | en_US | |
dc.publisher | National Academy of Sciences | |
dash.license | LAA | |
dc.title | A base-excision DNA-repair protein finds intrahelical lesion bases by fast sliding in contact with DNA | |
dc.type | Journal Article | |
dc.description.version | Version of Record | |
dc.relation.journal | Proceedings of the National Academy of Sciences of the United States of America | |
dash.depositing.author | Verdine, Gregory L.::b80a6eb8a9fb2d98773ce5b5cc1dd993::600 | |
dc.date.available | 2019-10-09T13:57:06Z | |
dash.workflow.comments | 1Science Serial ID 92931 | |
dc.identifier.doi | 10.1073/pnas.0509723103 | |
dash.source.volume | 103;15 | |
dash.source.page | 5752 | |