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Journal ArticleDOI

Mutagenic repair in Escherichia coli. X. The umuC gene product may be required for replication past pyrimidine dimers but not for the coding error in UV-mutagenesis.

Bryn A. Bridges, +1 more
- 01 Jan 1984 - 
- Vol. 196, Iss: 2, pp 364-366
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TLDR
In this article, it is suggested that base pair errors can be made opposite sites of pyrimidine dimers without involvement of umuC gene product but that the latter is required for continued replication past the dimermismatch region.
Abstract
Bacteria of strain TK610 uvrA-6 his-4 umuC-36, when allowed to replicate their DNA for some hours after irradiation show induction of His+ mutations when subsequently exposed to visible light. It is suggested that base pair errors can be made opposite sites of pyrimidine dimers without involvement of umuC gene product but that the latter is required for continued replication past the dimermismatch region. Removal of the pyrimidine dimer by photoreversal allows replication to continue thus fixing the mismatched base as as mutation.

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Citations
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Translesion DNA Polymerases

TL;DR: Despite being tightly regulated by a variety of transcriptional and posttranslational controls, the low-fidelity TLS polymerases also gain access to undamaged DNA where their inaccurate synthesis may actually be beneficial for genetic diversity and evolutionary fitness.
Journal ArticleDOI

Biochemical basis of SOS-induced mutagenesis in Escherichia coli: Reconstitution of in vitro lesion bypass dependent on the UmuD′2C mutagenic complex and RecA protein

TL;DR: Observations provide a biochemical basis for the role of the Umu complex in SOS-targeted and SOS-untargeted mutagenesis and its ability to stimulate both nucleotide misincorporation and mismatch extension at aberrant and normal template sites.
Journal ArticleDOI

Levels of chromosomally encoded Umu proteins and requirements for in vivo UmuD cleavage.

TL;DR: This paper found that the derepression of additional SOS gene products, other than RecA, was not required for UmuD processing, suggesting that efficient processing would occur only under conditions of severe DNA damage.
Journal ArticleDOI

Mutagenesis and More: umuDC and the Escherichia coli SOS Response

TL;DR: Investigations of the mechanisms underlying SOS mutagenesis, as well as recent observations suggesting that the umuDC operon may have a role in the regulation of the E. coli cell cycle after DNA damage has occurred, are discussed.
Journal ArticleDOI

The active form of DNA polymerase V is UmuD′ 2 C–RecA–ATP

TL;DR: The principal role of RecA* in SOS mutagenesis is to transfer RecA–ATP to pol V, and thus generate active mutasomal complex for translesion synthesis.
References
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Journal ArticleDOI

Mutants of escherichia coli requiring methionine or vitamin b12

TL;DR: Certain biochemical properties of auxotrophicl mutants of Escherichia coli with specific growth requirements for most of the known water-soluble vitamins, as well as of others responding to methionine but not to B,2 are described.
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Mutagenesis and inducible responses to deoxyribonucleic acid damage in Escherichia coli.

TL;DR: Comparing the SOS, Heat Shock, and Adaptive Regulatory Systems and evidence suggesting that UV mutagenesis does not require the induction of genes other than those repressed by LexA, the role of SOS processing to the spontaneous mutation frequency is suggested.
Journal ArticleDOI

Ultraviolet mutagenesis and inducible DNA repair in Escherichia coli.

TL;DR: This work states that the "SOS" Hypothesis, the Regulatory Role of DNA Damage in E. coli, and the Mechanism of SOS Repair in Bacteria and other UV-INDUCIBLE FUNCTIONS, and Regulations of SOS REPAIR, are valid hypotheses for the regulation of SOS functions.
Journal ArticleDOI

Isolation and characterization of mutants of Escherichia coli deficient in induction of mutations by ultraviolet light.

TL;DR: The mutation diminishes UV mutagenesis and UV reactivation of phages λ without affecting the inducibility of phophage λ nor the inhibition of cell division following UV irradiation.
Journal ArticleDOI

Cleavage of the Escherichia coli lexA protein by the recA protease.

TL;DR: Evidence is presented that the specific protease activity of the recA protein, previously described with the lambda repressor as substrate, is capable of cleaving the wild-type lexA+ protein and models for recA derepression and re-establishment of repression are discussed, which propose that modulation of the prote enzyme activity of recAprotein regulates both of these transitions.
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