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Protein FULL name:

G/U mismatch-specific DNA glycosylase [Escherichia coli str. K-12 substr. MG1655].

Mug (Escherichia coli strain K-12 substr. MG1655) is product of expression of mug gene.

Mug is involved in:

BER in Escherichia coli strain K-12 substr. MG1655


FUNCTION: Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells.

CATALYTIC ACTIVITY: Specifically hydrolyzes mismatched double- stranded DNA and polynucleotides, releasing free uracil.

ENZYME REGULATION: Subject to strong product inhibition. N- glycosyl hydrolysis proceeds 100-fold faster than product release.

SUBUNIT: Binds DNA as a monomer.

SUBCELLULAR LOCATION: Cytoplasm (Potential).

INDUCTION: Induced in stationary phase.

SIMILARITY: Belongs to the TDG/mug DNA glycosylase family.

NCBI GenPept GI number(s): 1789449
Species: Escherichia coli

Links to other databases:

Database ID Link
Uniprot P0A9H1 P0A9H1
PFAM: - P0A9H1 (Link - using uniprot id)
InterPro: - P0A9H1 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -

Protein sequence:

Mug (Escherichia coli strain K-12 substr. MG1655) is able to recognize following damages:

Title Authors Journal
The nucleotide sequence of the cloned rpoD gene for the RNA polymerase sigma subunit from E coli K12. Burton Z, Burgess RR, Lin J, Moore D, Holder S, Gross CA Nucleic Acids Res June 25, 1981
Detection of new genes in a bacterial genome using Markov models for three gene classes. Borodovsky M, McIninch JD, Koonin EV, Rudd KE, Medigue C, Danchin A Nucleic Acids Res Sept. 11, 1995
A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase. Gallinari P, Jiricny J Nature Oct. 24, 1996
The complete genome sequence of Escherichia coli K-12. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y Science Sept. 5, 1997
Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Barrett TE, Savva R, Panayotou G, Barlow T, Brown T, Jiricny J, Pearl LH Cell Feb. 9, 1998
Structure of a DNA base-excision product resembling a cisplatin inter-strand adduct. Barrett TE, Savva R, Barlow T, Brown T, Jiricny J, Pearl LH Nat Struct Biol Aug. 1, 1998
Crystal structure of a thwarted mismatch glycosylase DNA repair complex. Barrett TE, Scharer OD, Savva R, Brown T, Jiricny J, Verdine GL, Pearl LH EMBO J Dec. 1, 1999
Escherichia coli DNA glycosylase Mug: a growth-regulated enzyme required for mutation avoidance in stationary-phase cells. Mokkapati SK, Fernandez de Henestrosa AR, Bhagwat AS Mol Microbiol Sept. 1, 2001
Mismatch uracil glycosylase from Escherichia coli: a general mismatch or a specific DNA glycosylase? O'Neill RJ, Vorob'eva OV, Shahbakhti H, Zmuda E, Bhagwat AS, Baldwin GS J Biol Chem June 6, 2003
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T Mol Syst Biol Jan. 1, 2006

Last modification of this entry: Oct. 13, 2010.

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