Distinct substrate preference of human and mouse N-methylpurine-DNA glycosylases

Rabindra Roy, Stephen Kennel, Sankar Mitra

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

N-Methylpurine-DNA glycosylase (MPG), a ubiquitous DNA repair protein, removes several N-alkylpurine adducts, hypoxanthine, cyclic ethenoadducts of adenine, guanine and cytosine and 8-oxoguanine from DNA. The recombinant human and mouse MPGs, purified from Escherichia coli, show a significant difference in substrate preference. While both proteins prefer 3-methyladenine over other N-alkylpurines in DNA, the mouse MPG removes 7-methylguanine and 3-methylguanine at an ~2- to 3-fold higher rate than the human protein when adjusted for equal activity for the release of 3-methyladenine from DNA. Hybrid recombinant proteins containing N-terminal and C-terminal halves of the human and mouse glycosylases were partially purified from MPG-negative E.coli. Their substrate preferences suggest that the N-terminal half is more critical for the recognition of 3-methylguanine and 7-methylguanine.

Original languageEnglish (US)
Pages (from-to)2177-2182
Number of pages6
JournalCarcinogenesis
Volume17
Issue number10
DOIs
StatePublished - Oct 1 1996

Fingerprint

DNA
Recombinant Fusion Proteins
Escherichia coli
Proteins
Hypoxanthine
Cytosine
Guanine
Adenine
DNA Repair
DNA-3-methyladenine glycosidase II
3-methylguanine
7-methylguanine
3-methyladenine
8-hydroxyguanine

All Science Journal Classification (ASJC) codes

  • Cancer Research

Cite this

Distinct substrate preference of human and mouse N-methylpurine-DNA glycosylases. / Roy, Rabindra; Kennel, Stephen; Mitra, Sankar.

In: Carcinogenesis, Vol. 17, No. 10, 01.10.1996, p. 2177-2182.

Research output: Contribution to journalArticle

Roy, Rabindra ; Kennel, Stephen ; Mitra, Sankar. / Distinct substrate preference of human and mouse N-methylpurine-DNA glycosylases. In: Carcinogenesis. 1996 ; Vol. 17, No. 10. pp. 2177-2182.
@article{35dac59f92284270a7acfbf4441c43e8,
title = "Distinct substrate preference of human and mouse N-methylpurine-DNA glycosylases",
abstract = "N-Methylpurine-DNA glycosylase (MPG), a ubiquitous DNA repair protein, removes several N-alkylpurine adducts, hypoxanthine, cyclic ethenoadducts of adenine, guanine and cytosine and 8-oxoguanine from DNA. The recombinant human and mouse MPGs, purified from Escherichia coli, show a significant difference in substrate preference. While both proteins prefer 3-methyladenine over other N-alkylpurines in DNA, the mouse MPG removes 7-methylguanine and 3-methylguanine at an ~2- to 3-fold higher rate than the human protein when adjusted for equal activity for the release of 3-methyladenine from DNA. Hybrid recombinant proteins containing N-terminal and C-terminal halves of the human and mouse glycosylases were partially purified from MPG-negative E.coli. Their substrate preferences suggest that the N-terminal half is more critical for the recognition of 3-methylguanine and 7-methylguanine.",
author = "Rabindra Roy and Stephen Kennel and Sankar Mitra",
year = "1996",
month = "10",
day = "1",
doi = "10.1093/carcin/17.10.2177",
language = "English (US)",
volume = "17",
pages = "2177--2182",
journal = "Carcinogenesis",
issn = "0143-3334",
publisher = "Oxford University Press",
number = "10",

}

TY - JOUR

T1 - Distinct substrate preference of human and mouse N-methylpurine-DNA glycosylases

AU - Roy, Rabindra

AU - Kennel, Stephen

AU - Mitra, Sankar

PY - 1996/10/1

Y1 - 1996/10/1

N2 - N-Methylpurine-DNA glycosylase (MPG), a ubiquitous DNA repair protein, removes several N-alkylpurine adducts, hypoxanthine, cyclic ethenoadducts of adenine, guanine and cytosine and 8-oxoguanine from DNA. The recombinant human and mouse MPGs, purified from Escherichia coli, show a significant difference in substrate preference. While both proteins prefer 3-methyladenine over other N-alkylpurines in DNA, the mouse MPG removes 7-methylguanine and 3-methylguanine at an ~2- to 3-fold higher rate than the human protein when adjusted for equal activity for the release of 3-methyladenine from DNA. Hybrid recombinant proteins containing N-terminal and C-terminal halves of the human and mouse glycosylases were partially purified from MPG-negative E.coli. Their substrate preferences suggest that the N-terminal half is more critical for the recognition of 3-methylguanine and 7-methylguanine.

AB - N-Methylpurine-DNA glycosylase (MPG), a ubiquitous DNA repair protein, removes several N-alkylpurine adducts, hypoxanthine, cyclic ethenoadducts of adenine, guanine and cytosine and 8-oxoguanine from DNA. The recombinant human and mouse MPGs, purified from Escherichia coli, show a significant difference in substrate preference. While both proteins prefer 3-methyladenine over other N-alkylpurines in DNA, the mouse MPG removes 7-methylguanine and 3-methylguanine at an ~2- to 3-fold higher rate than the human protein when adjusted for equal activity for the release of 3-methyladenine from DNA. Hybrid recombinant proteins containing N-terminal and C-terminal halves of the human and mouse glycosylases were partially purified from MPG-negative E.coli. Their substrate preferences suggest that the N-terminal half is more critical for the recognition of 3-methylguanine and 7-methylguanine.

UR - http://www.scopus.com/inward/record.url?scp=0029829188&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029829188&partnerID=8YFLogxK

U2 - 10.1093/carcin/17.10.2177

DO - 10.1093/carcin/17.10.2177

M3 - Article

VL - 17

SP - 2177

EP - 2182

JO - Carcinogenesis

JF - Carcinogenesis

SN - 0143-3334

IS - 10

ER -