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

Gene ID: 946765, updated on 3-Dec-2024

Summary

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Official Symbol
mutM
Official Full Name
DNA-formamidopyrimidine glycosylase
Primary source
ECOCYC:EG10329
Locus tag
b3635
See related
ASAP:ABE-0011877
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_000913.3Genomic Context describing neighboring genes Neighboring gene KDO transferase Neighboring gene pantetheine-phosphate adenylyltransferase Neighboring gene 50S ribosomal subunit protein L33 Neighboring gene 50S ribosomal subunit protein L28

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Overexpression and rapid purification of Escherichia coli formamidopyrimidine-DNA glycosylase. Reddy P, et al. Protein Expr Purif, 2004 Mar. PMID 14766308
  2. Accelerated repair and reduced mutagenicity of oxidative DNA damage in human bladder cells expressing the E. coli FPG protein. Ropolo M, et al. Int J Cancer, 2006 Apr 1. PMID 16217765
  3. Thermodynamic, kinetic, and structural basis for recognition and repair of 8-oxoguanine in DNA by Fpg protein from Escherichia coli. Ishchenko AA, et al. Biochemistry, 2002 Jun 18. PMID 12056884
  4. Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein. Boiteux S, et al. EMBO J, 1987 Oct. PMID 3319582, Free PMC Article
  5. Recognition of oxidized abasic sites by repair endonucleases. Häring M, et al. Nucleic Acids Res, 1994 Jun 11. PMID 7518077, Free PMC Article

See all (118) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.
  9. 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.
  10. 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.
Submit: New GeneRIF Correction See all GeneRIFs (18)

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

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

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

  1. NC_000913.3 Reference assembly

    Range
    3810343..3811152 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. 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
Nucleotide Protein
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