2010
DOI: 10.1074/jbc.m110.115774
|View full text |Cite
|
Sign up to set email alerts
|

UmuD2 Inhibits a Non-covalent Step during DinB-mediated Template Slippage on Homopolymeric Nucleotide Runs

Abstract: Escherichia coli DinB (DNA polymerase IV) possesses an enzyme architecture resulting in specialized lesion bypass function and the potential for creating ؊1 frameshifts in homopolymeric nucleotide runs. We have previously shown that the mutagenic potential of DinB is regulated by the DNA damage response protein UmuD 2 . In the current study, we employ a presteady-state fluorescence approach to gain a mechanistic understanding of DinB regulation by UmuD 2 . Our results suggest that DinB, like its mammalian and … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

1
24
0

Year Published

2011
2011
2021
2021

Publication Types

Select...
6
1
1

Relationship

0
8

Authors

Journals

citations
Cited by 20 publications
(25 citation statements)
references
References 40 publications
(90 reference statements)
1
24
0
Order By: Relevance
“…Although all Acinetobacter strains possess a dinP gene, only A. ursingii possesses a umuD-dinP locus, raising the possibility that this unique locus might be associated with its capacity to conduct UV-induced mutagenesis. The UmuD 2 homodimer can interact with DinP (DNA pol IV), and alter its mutagenic activity in E. coli (Foti et al, 2010;Godoy et al, 2007). Supporting this possibility is the distinctiveness of this dinP-linked umuD allele, as strongly supported by bootstrap analysis (Fig.…”
supporting
confidence: 48%
See 1 more Smart Citation
“…Although all Acinetobacter strains possess a dinP gene, only A. ursingii possesses a umuD-dinP locus, raising the possibility that this unique locus might be associated with its capacity to conduct UV-induced mutagenesis. The UmuD 2 homodimer can interact with DinP (DNA pol IV), and alter its mutagenic activity in E. coli (Foti et al, 2010;Godoy et al, 2007). Supporting this possibility is the distinctiveness of this dinP-linked umuD allele, as strongly supported by bootstrap analysis (Fig.…”
supporting
confidence: 48%
“…Two cleaved UmuD9 molecules then associate with UmuC to form DNA polymerase V, which carries out error-prone, trans-lesion DNA replication (SOS mutagenesis) (Reuven et al, 1999;Tang et al, 1999). Another errorprone polymerase commonly involved in SOS mutagenesis as part of the DNA damage response is DinP (also called DinB), DNA polymerase IV, which can function either by itself (Kim et al, 1997) or with UmuD (Foti et al, 2010;Godoy et al, 2007).…”
Section: Introductionmentioning
confidence: 99%
“…We conclude from the data presented here that Dpo4 uses a template slippage mechanism when making single-base deletion mutations in repetitive DNA sequences. Previous work on Dbh (6, 31) and E. coli DinB (10) indicates that they also use a template slippage mechanism. The archaeal and bacterial DinB polymerases, therefore, share a conserved mechanism when copying the kinds of repetitive sequences in which deletions most frequently occur.…”
Section: Discussionmentioning
confidence: 99%
“…Dbh has been shown to use a template slippage mechanism (6,31), while Dpo4 has been proposed to use dNTP-stabilized misalignment (9,12,16). Earlier experiments indicated that DinB from Escherichia coli used a dNTP-stabilized misalignment mechanism (28), although more recent work shows that it uses a template slippage mechanism (10). Human polymerase kappa can use a misinsertion-misalignment mechanism in nonrepetitive sequences, while template slippage has been inferred as the mechanism used in repetitive sequences (20,32).…”
mentioning
confidence: 99%
“…However, with the assistance of the β-clamp, the processivity of pol IV increases by 2-to 4-orders of magnitude enabling it to synthesize over 1 kb DNA (241). Recently, it has been suggested that UmuD physically interacts with Pol IV (85) and in doing so, helps cap the polymerase's active site, so as to increase pol IVs fidelity (71,85).…”
Section: Cofactor Requirements That Modify the Fidelity And Processivmentioning
confidence: 99%