Action mechanism of human SMUG1 uracil-DNA glycosylase.

Mayumi Matsubara; Tamon Tanaka; Hiroaki Terato; Hiroshi Ide

doi:10.1093/nass/49.1.295

Action mechanism of human SMUG1 uracil-DNA glycosylase.

Mayumi Matsubara, Tamon Tanaka, Hiroaki Terato, Hiroshi Ide

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

The DNA lesions resulting from deamination or oxidation of bases are generally repaired by the base excision repair pathway initiated by damage-specific DNA glycosylases. Single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) present in vertebrates and insects excises not only uracil but also uracil derivatives bearing an oxidized group at ring-C5 from DNA, indicating roles in the repair of both deamination and oxidation damage to DNA. In the present study, we have constructed a series of active site mutants of human SMUG1 and analyzed the catalytic and precision damage recognition mechanisms.

Original language	English
Pages (from-to)	295-296
Number of pages	2
Journal	Nucleic acids symposium series (2004)
Issue number	49
DOIs	https://doi.org/10.1093/nass/49.1.295
Publication status	Published - 2005
Externally published	Yes

ASJC Scopus subject areas

Medicine(all)

Access to Document

10.1093/nass/49.1.295

Cite this

@article{331af57c37e64ec1ba10dfc2d2056947,

title = "Action mechanism of human SMUG1 uracil-DNA glycosylase.",

abstract = "The DNA lesions resulting from deamination or oxidation of bases are generally repaired by the base excision repair pathway initiated by damage-specific DNA glycosylases. Single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) present in vertebrates and insects excises not only uracil but also uracil derivatives bearing an oxidized group at ring-C5 from DNA, indicating roles in the repair of both deamination and oxidation damage to DNA. In the present study, we have constructed a series of active site mutants of human SMUG1 and analyzed the catalytic and precision damage recognition mechanisms.",

author = "Mayumi Matsubara and Tamon Tanaka and Hiroaki Terato and Hiroshi Ide",

year = "2005",

doi = "10.1093/nass/49.1.295",

language = "English",

pages = "295--296",

journal = "Nucleic acids symposium series (2004)",

issn = "1746-8272",

publisher = "Oxford University Press",

number = "49",

}

TY - JOUR

T1 - Action mechanism of human SMUG1 uracil-DNA glycosylase.

AU - Matsubara, Mayumi

AU - Tanaka, Tamon

AU - Terato, Hiroaki

AU - Ide, Hiroshi

PY - 2005

Y1 - 2005

N2 - The DNA lesions resulting from deamination or oxidation of bases are generally repaired by the base excision repair pathway initiated by damage-specific DNA glycosylases. Single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) present in vertebrates and insects excises not only uracil but also uracil derivatives bearing an oxidized group at ring-C5 from DNA, indicating roles in the repair of both deamination and oxidation damage to DNA. In the present study, we have constructed a series of active site mutants of human SMUG1 and analyzed the catalytic and precision damage recognition mechanisms.

AB - The DNA lesions resulting from deamination or oxidation of bases are generally repaired by the base excision repair pathway initiated by damage-specific DNA glycosylases. Single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) present in vertebrates and insects excises not only uracil but also uracil derivatives bearing an oxidized group at ring-C5 from DNA, indicating roles in the repair of both deamination and oxidation damage to DNA. In the present study, we have constructed a series of active site mutants of human SMUG1 and analyzed the catalytic and precision damage recognition mechanisms.

UR - http://www.scopus.com/inward/record.url?scp=39049194527&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=39049194527&partnerID=8YFLogxK

U2 - 10.1093/nass/49.1.295

DO - 10.1093/nass/49.1.295

M3 - Article

C2 - 17150750

AN - SCOPUS:39049194527

SN - 1746-8272

SP - 295

EP - 296

JO - Nucleic acids symposium series (2004)

JF - Nucleic acids symposium series (2004)

IS - 49

ER -

Action mechanism of human SMUG1 uracil-DNA glycosylase.

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this