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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
    Heading Accession and Version

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