mutM DNA-formamidopyrimidine glycosylase [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Gene symbol: mutM
Gene description: DNA-formamidopyrimidine glycosylase
Primary source: ASAP:ABE-0011877
Locus tag: b3635
See related: ECOCYC:EG10329
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK3625; fpg
Summary: MutM (also known as Fpg) is a DNA glycosylase that works in the base excision repair (BER) pathway to repair certain types of pre-mutagenic lesions. [More information is available at EcoCyc: EG10329].
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Genomic context

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Sequence:: NC_000913.3 (3810343..3811152, complement)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Requirements for DNA bubble structure for efficient cleavage by helix-two-turn-helix DNA glycosylases.
Title: Requirements for DNA bubble structure for efficient cleavage by helix-two-turn-helix DNA glycosylases.
Through DNA binding, the two proteins interplay to form a transient ternary complex Fpg/DNA/HU which results in the release of Fpg and the molecular entrapment of SSBs by HU
Title: The nucleoid-associated protein HU enhances 8-oxoguanine base excision by the formamidopyrimidine-DNA glycosylase.
expression of the bacterial DNA repair protein FPG stably protects human lung cells from the mutagenic effects of CS by improving cells' capacity to repair damaged DNA.
Title: Accelerated repair and reduced mutagenicity of DNA damage induced by cigarette smoke in human bronchial cells transfected with E.coli formamidopyrimidine DNA glycosylase.
Structural and biochemical analysis of DNA helix invasion by the bacterial 8-oxoguanine DNA glycosylase MutM
Title: Structural and biochemical analysis of DNA helix invasion by the bacterial 8-oxoguanine DNA glycosylase MutM.
Fpg protein seemed to be very important in the repair of ultraviolet-C induced DNA lesions.
Title: The role of Fpg protein in UVC-induced DNA lesions.
structures reveal that MutM imposes the same extrusion-prone backbone conformation on the oxoG lesion irrespective of its 5'-neighbor while leaving the rest of the DNA relatively free to adjust to the particular demands of individual sequences
Title: Sequence-dependent structural variation in DNA undergoing intrahelical inspection by the DNA glycosylase MutM.
demonstrates that it is feasible to increase resistance of human TM cell to endogenous oxidative damage by FPG gene transfection
Title: Increased resistance to oxidative DNA damage of trabecular meshwork cells by E. coli FPG gene transfection.
Over-expressed, purified and characterized two stable isotope-labeled DNA glycosylases, i.e., (15)N-labeled Escherichia coli formamidopyrimidine DNA glycosylase (Fpg) and (15)N-labeled human 8-oxoguanine-DNA glycosylase (hOGG1).
Title: Stable isotope-labeling of DNA repair proteins, and their purification and characterization.
Data show that processive cleavage by Fpg does not correlate with their substrate specificity and under nearly physiological salt conditions may be replaced with the distributive mode of action.
Title: Correlated cleavage of damaged DNA by bacterial and human 8-oxoguanine-DNA glycosylases.
Data show a lack of interaction of mutM with dnaX36 since the double dnaX36 mutM strains did not show any major changes in the frequency of G.CT.A transversions compared to the single dnaX36 strain.
Title: Role of accessory DNA polymerases in DNA replication in Escherichia coli: analysis of the dnaX36 mutator mutant.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity	IBA Inferred from Biological aspect of Ancestor more info
enables 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity	IDA Inferred from Direct Assay more info	PubMed
enables 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables DNA N-glycosylase activity	EXP Inferred from Experiment more info	PubMed
enables DNA N-glycosylase activity	IDA Inferred from Direct Assay more info	PubMed
enables DNA binding	IEA Inferred from Electronic Annotation more info
enables DNA-(apurinic or apyrimidinic site) endonuclease activity	IBA Inferred from Biological aspect of Ancestor more info
enables DNA-(apurinic or apyrimidinic site) endonuclease activity	IDA Inferred from Direct Assay more info	PubMed
enables DNA-(apurinic or apyrimidinic site) endonuclease activity	IEA Inferred from Electronic Annotation more info
enables class I DNA-(apurinic or apyrimidinic site) endonuclease activity	IDA Inferred from Direct Assay more info	PubMed
enables class I DNA-(apurinic or apyrimidinic site) endonuclease activity	IEA Inferred from Electronic Annotation more info
enables damaged DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables damaged DNA binding	IEA Inferred from Electronic Annotation more info
enables endonuclease activity	EXP Inferred from Experiment more info	PubMed
enables endonuclease activity	IDA Inferred from Direct Assay more info	PubMed
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables hydrolase activity, acting on glycosyl bonds	IEA Inferred from Electronic Annotation more info
enables lyase activity	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IDA Inferred from Direct Assay more info	PubMed
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables oxidized purine nucleobase lesion DNA N-glycosylase activity	IDA Inferred from Direct Assay more info	PubMed
enables oxidized purine nucleobase lesion DNA N-glycosylase activity	IEA Inferred from Electronic Annotation more info
enables oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within DNA damage response	IDA Inferred from Direct Assay more info	PubMed
involved_in DNA repair	IEA Inferred from Electronic Annotation more info
involved_in base-excision repair	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within base-excision repair	IDA Inferred from Direct Assay more info	PubMed
involved_in base-excision repair	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within base-excision repair	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IC Inferred by Curator more info	PubMed

General protein information

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Preferred Names: DNA-formamidopyrimidine glycosylase

NP_418092.1

EC 3.2.2.23

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

3810343..3811152 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_418092.1 DNA-formamidopyrimidine glycosylase [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_418092.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A7D7P6Z8

Conserved Domains (1) summary

PRK01103
Location:1 → 269

PRK01103; bifunctional DNA-formamidopyrimidine glycosylase/DNA-(apurinic or apyrimidinic site) lyase