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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
Keywords:
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.
Links to other databases:
Protein sequence:
MVEDILAPGLRVVFCGINPGLSSAGTGFPFAHPANRFWKVIYQAGFTDRQ
LKPQEAQHLLDYRCGVTKLVDRPTVQANEVSKQELHAGGRKLIEKIEDYQ
PQALAILGKQAYEQGFSQRGAQWGKQTLTIGSTQIWVLPNPSGLSRVSLE
KLVEAYRELDQALVVRGR
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Mug (Escherichia coli strain K-12 substr. MG1655) is able to recognize following damages:
References:
Title
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Authors
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Journal
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The nucleotide sequence of the cloned rpoD gene for the RNA polymerase sigma subunit from E coli K12.
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Burton Z, Burgess RR, Lin J, Moore D, Holder S, Gross CA
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Nucleic Acids Res
June 25, 1981
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Detection of new genes in a bacterial genome using Markov models for three gene classes.
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Borodovsky M, McIninch JD, Koonin EV, Rudd KE, Medigue C, Danchin A
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Nucleic Acids Res
Sept. 11, 1995
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A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase.
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Gallinari P, Jiricny J
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Nature
Oct. 24, 1996
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The complete genome sequence of Escherichia coli K-12.
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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
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Science
Sept. 5, 1997
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Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions.
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Barrett TE, Savva R, Panayotou G, Barlow T, Brown T, Jiricny J, Pearl LH
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Cell
Feb. 9, 1998
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Structure of a DNA base-excision product resembling a cisplatin inter-strand adduct.
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Barrett TE, Savva R, Barlow T, Brown T, Jiricny J, Pearl LH
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Nat Struct Biol
Aug. 1, 1998
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Crystal structure of a thwarted mismatch glycosylase DNA repair complex.
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Barrett TE, Scharer OD, Savva R, Brown T, Jiricny J, Verdine GL, Pearl LH
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EMBO J
Dec. 1, 1999
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Escherichia coli DNA glycosylase Mug: a growth-regulated enzyme required for mutation avoidance in stationary-phase cells.
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Mokkapati SK, Fernandez de Henestrosa AR, Bhagwat AS
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Mol Microbiol
Sept. 1, 2001
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Mismatch uracil glycosylase from Escherichia coli: a general mismatch or a specific DNA glycosylase?
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O'Neill RJ, Vorob'eva OV, Shahbakhti H, Zmuda E, Bhagwat AS, Baldwin GS
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J Biol Chem
June 6, 2003
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Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
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Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T
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Mol Syst Biol
Jan. 1, 2006
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Last modification of this entry: Oct. 13, 2010.
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