Matches in SemOpenAlex for { <https://semopenalex.org/work/W2068700915> ?p ?o ?g. }
Showing items 1 to 69 of
69
with 100 items per page.
- W2068700915 endingPage "342a" @default.
- W2068700915 startingPage "341a" @default.
- W2068700915 abstract "The Y family of DNA polymerases is a group of DNA damage tolerance enzymes with the specialized ability to bypass DNA lesions by inserting nucleotides opposite damaged sites in DNA. Translesion synthesis (TLS) responsible for most of the mutagenesis induced by UV radiation requires the UmuD'2 protein (the cleaved form of the UmuD2), UmuC, and RecA. UmuD'2 activates UmuC, the catalytic subunit of the Y family DNA polymerase V, for mutagenic DNA replication. UmuD2 and UmuD'2 make a remarkable number of specific protein-protein contacts to DNA polymerases. Despite the nearly identical primary structure of UmuD2 and UmuD'2, their interactions with the same partner can differ in affinity and functional significance. Analysis of the UmuD/UmuD'-pol III interactions by affinity chromatography indicated that UmuD has a lower affinity for alpha (α) subunit of E. coli’s replicative polymerase III than does UmuD'. We aim to understand how binding of UmuD dimers is coordinated with the activity of α subunit. We are utilizing the biochemical and biophysical methods to look at the kinetics of α subunit activity and at the formation of α-UmuD2 and α-UmuD'2 complexes. We are characterizing the ability of the α subunit to copy both damaged and undamaged DNA in the presence of UmuD and UmuD'. In order to quantify the binding of UmuD and UmuD' to the α subunit, we are determining the Kd (equilibrium dissociation constant) for this interaction by measuring intrinsic tryptophan fluorescence of the α subunit." @default.
- W2068700915 created "2016-06-24" @default.
- W2068700915 creator A5015910317 @default.
- W2068700915 creator A5021306241 @default.
- W2068700915 creator A5056925655 @default.
- W2068700915 creator A5062695629 @default.
- W2068700915 date "2009-02-01" @default.
- W2068700915 modified "2023-10-18" @default.
- W2068700915 title "Quantitative Characterization of Interactions of the Escherichia Coli SOS DNA Damage Response Proteins UmuD and UmuD' with the Replicative DNA Polymerase" @default.
- W2068700915 doi "https://doi.org/10.1016/j.bpj.2008.12.1714" @default.
- W2068700915 hasPublicationYear "2009" @default.
- W2068700915 type Work @default.
- W2068700915 sameAs 2068700915 @default.
- W2068700915 citedByCount "0" @default.
- W2068700915 crossrefType "journal-article" @default.
- W2068700915 hasAuthorship W2068700915A5015910317 @default.
- W2068700915 hasAuthorship W2068700915A5021306241 @default.
- W2068700915 hasAuthorship W2068700915A5056925655 @default.
- W2068700915 hasAuthorship W2068700915A5062695629 @default.
- W2068700915 hasBestOaLocation W20687009151 @default.
- W2068700915 hasConcept C104292427 @default.
- W2068700915 hasConcept C104317684 @default.
- W2068700915 hasConcept C143425029 @default.
- W2068700915 hasConcept C153911025 @default.
- W2068700915 hasConcept C156719811 @default.
- W2068700915 hasConcept C2756471 @default.
- W2068700915 hasConcept C2780852648 @default.
- W2068700915 hasConcept C31254050 @default.
- W2068700915 hasConcept C49105822 @default.
- W2068700915 hasConcept C552990157 @default.
- W2068700915 hasConcept C55493867 @default.
- W2068700915 hasConcept C73573662 @default.
- W2068700915 hasConcept C82381507 @default.
- W2068700915 hasConcept C86803240 @default.
- W2068700915 hasConceptScore W2068700915C104292427 @default.
- W2068700915 hasConceptScore W2068700915C104317684 @default.
- W2068700915 hasConceptScore W2068700915C143425029 @default.
- W2068700915 hasConceptScore W2068700915C153911025 @default.
- W2068700915 hasConceptScore W2068700915C156719811 @default.
- W2068700915 hasConceptScore W2068700915C2756471 @default.
- W2068700915 hasConceptScore W2068700915C2780852648 @default.
- W2068700915 hasConceptScore W2068700915C31254050 @default.
- W2068700915 hasConceptScore W2068700915C49105822 @default.
- W2068700915 hasConceptScore W2068700915C552990157 @default.
- W2068700915 hasConceptScore W2068700915C55493867 @default.
- W2068700915 hasConceptScore W2068700915C73573662 @default.
- W2068700915 hasConceptScore W2068700915C82381507 @default.
- W2068700915 hasConceptScore W2068700915C86803240 @default.
- W2068700915 hasIssue "3" @default.
- W2068700915 hasLocation W20687009151 @default.
- W2068700915 hasOpenAccess W2068700915 @default.
- W2068700915 hasPrimaryLocation W20687009151 @default.
- W2068700915 hasRelatedWork W1932201017 @default.
- W2068700915 hasRelatedWork W1969663477 @default.
- W2068700915 hasRelatedWork W1985206061 @default.
- W2068700915 hasRelatedWork W1996629794 @default.
- W2068700915 hasRelatedWork W2029169816 @default.
- W2068700915 hasRelatedWork W2068700915 @default.
- W2068700915 hasRelatedWork W2139492238 @default.
- W2068700915 hasRelatedWork W2164303657 @default.
- W2068700915 hasRelatedWork W2259828804 @default.
- W2068700915 hasRelatedWork W2527050327 @default.
- W2068700915 hasVolume "96" @default.
- W2068700915 isParatext "false" @default.
- W2068700915 isRetracted "false" @default.
- W2068700915 magId "2068700915" @default.
- W2068700915 workType "article" @default.