Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2186924 | Journal of Molecular Biology | 2009 | 18 Pages |
Abstract
SummarySliding clamp proteins topologically encircle DNA and play vital roles in coordinating the actions of various DNA replication, repair, and damage tolerance proteins. At least three distinct surfaces of the Escherichia coli β clamp interact physically with the DNA that it topologically encircles. We utilized mutant β clamp proteins bearing G66E and G174A substitutions (β159), affecting the single-stranded DNA-binding region, or poly-Ala substitutions in place of residues 148-HQDVR-152 (β148–152), affecting the double-stranded DNA binding region, to determine the biological relevance of
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Authors
Justin M.H. Heltzel, Sarah K. Scouten Ponticelli, Laurie H. Sanders, Jill M. Duzen, Vivian Cody, James Pace, Edward H. Snell, Mark D. Sutton,