Journal
NUCLEIC ACIDS RESEARCH
Volume 41, Issue 19, Pages 8959-8968Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkt648
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Funding
- National Institutes of Health [GM072462]
- National Science Foundation [MCB-1243883, MCB-0845033]
- American Cancer Society Research Scholar Grant [RSG-12-161-01-DMC]
- NU Office of the Provost
- National Science Foundation [ROA supplement] [MCB-1243883]
- NSF IGERT Program [DGE-0504331]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1243883] Funding Source: National Science Foundation
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0845033] Funding Source: National Science Foundation
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Replication by Escherichia coli DNA polymerase III is disrupted on encountering DNA damage. Consequently, specialized Y-family DNA polymerases are used to bypass DNA damage. The protein UmuD is extensively involved in modulating cellular responses to DNA damage and may play a role in DNA polymerase exchange for damage tolerance. In the absence of DNA, UmuD interacts with the alpha subunit of DNA polymerase III at two distinct binding sites, one of which is adjacent to the single-stranded DNA-binding site of alpha. Here, we use single molecule DNA stretching experiments to demonstrate that UmuD specifically inhibits binding of alpha to ssDNA. We predict using molecular modeling that UmuD residues D91 and G92 are involved in this interaction and demonstrate that mutation of these residues disrupts the interaction. Our results suggest that competition between UmuD and ssDNA for alpha binding is a new mechanism for polymerase exchange.
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