A non-cleavable UmuD variant that acts as a UmuD′ mimic. VOLUME 281 (2006) PAGES 9633-9640
Year: 2006
Type: article
Abstract: A Non-cleavable UmuD Variant That Acts as a UmuD′ MimicJournal of Biological ChemistryVol. 281Issue 14PreviewUmuD2 cleaves and removes its N-terminal 24 amino acids to form UmuD′2, which activates UmuC for its role in UV-induced mutagenesis in Escherichia coli. Cells with a non-cleavable UmuD exhibit essentially no UV-induced mutagenesis and are hypersensitive to killing by UV light. UmuD binds to the β processivity clamp (“β”) of the replicative DNA polymerase, pol III. A possible β-binding motif has been predicted in the same region of UmuD shown to be important for its interaction with β. We performed alanine-scanning mutagenesis of this motif (14TFPLF18) in UmuD and found that it has a moderate influence on UV-induced mutagenesis but is required for the cold-sensitive phenotype caused by elevated levels of wild-type UmuD and UmuC. Full-Text PDF Open Access PAGES 9634-9640: The symbol for “prime” was inadvertently left out of the running title. The running title should read: A UmuD Variant That Mimics UmuD′.
Source: Journal of Biological Chemistry
Language: English
Topic: DNA Repair Mechanisms
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1559820848