O6-Methylguanine-DNA methyltransferase in human cells

Daniel B. Yarosh; Mary Rice; Rufus S. Day; Robert S. Foote; Sankar Mitra

doi:10.1016/0167-8817(84)90044-0

O⁶-Methylguanine-DNA methyltransferase in human cells

Daniel B. Yarosh, Mary Rice, Rufus S. Day, Robert S. Foote, Sankar Mitra

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

79 Scopus citations

Abstract

O⁶-Methylguanine-DNA methyltransferase activity was measured in extracts of human tumor cells and was partially purified from human placenta. Repair of O⁶-methylguanine in DNA inactivated the methyltransferase, and treatment of cells with MNNG, which produces this alkylated base in DNA, depleted the cells of active methyltransferase. RNA and protein synthesis were required for restoration of methyltransferase activity, which transiently exceeded the original levels by 50% 48 h after treatment. One species of methyltransferase of M_r = 22 kd was present in human tumor cells and human placenta.

Original language	English (US)
Pages (from-to)	27-36
Number of pages	10
Journal	Mutation Research DNA Repair Reports
Volume	131
Issue number	1
DOIs	https://doi.org/10.1016/0167-8817(84)90044-0
State	Published - Jan 1984

ASJC Scopus subject areas

Molecular Biology
Health, Toxicology and Mutagenesis
General Medicine

Access to Document

10.1016/0167-8817(84)90044-0

Cite this

@article{383242d1615d418d8ec84ef6d8524d73,

title = "O6-Methylguanine-DNA methyltransferase in human cells",

abstract = "O6-Methylguanine-DNA methyltransferase activity was measured in extracts of human tumor cells and was partially purified from human placenta. Repair of O6-methylguanine in DNA inactivated the methyltransferase, and treatment of cells with MNNG, which produces this alkylated base in DNA, depleted the cells of active methyltransferase. RNA and protein synthesis were required for restoration of methyltransferase activity, which transiently exceeded the original levels by 50% 48 h after treatment. One species of methyltransferase of Mr = 22 kd was present in human tumor cells and human placenta.",

author = "Yarosh, {Daniel B.} and Mary Rice and Day, {Rufus S.} and Foote, {Robert S.} and Sankar Mitra",

note = "Funding Information: Thanks to Linda Nischan for manuscript preparation. R.S.F. and S.M. were supported by an N.C.I. contract Y02-CP-00200 to Oak Ridge National Laboratory and by the U.S. Department of Energy under contract W-7405-eng-26 with the Union Carbide Corporation. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "1984",

month = jan,

doi = "10.1016/0167-8817(84)90044-0",

language = "English (US)",

volume = "131",

pages = "27--36",

journal = "Mutation Research DNA Repair Reports",

issn = "0167-8817",

publisher = "Elsevier B.V.",

number = "1",

}

TY - JOUR

T1 - O6-Methylguanine-DNA methyltransferase in human cells

AU - Yarosh, Daniel B.

AU - Rice, Mary

AU - Day, Rufus S.

AU - Foote, Robert S.

AU - Mitra, Sankar

N1 - Funding Information: Thanks to Linda Nischan for manuscript preparation. R.S.F. and S.M. were supported by an N.C.I. contract Y02-CP-00200 to Oak Ridge National Laboratory and by the U.S. Department of Energy under contract W-7405-eng-26 with the Union Carbide Corporation. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 1984/1

Y1 - 1984/1

N2 - O6-Methylguanine-DNA methyltransferase activity was measured in extracts of human tumor cells and was partially purified from human placenta. Repair of O6-methylguanine in DNA inactivated the methyltransferase, and treatment of cells with MNNG, which produces this alkylated base in DNA, depleted the cells of active methyltransferase. RNA and protein synthesis were required for restoration of methyltransferase activity, which transiently exceeded the original levels by 50% 48 h after treatment. One species of methyltransferase of Mr = 22 kd was present in human tumor cells and human placenta.

AB - O6-Methylguanine-DNA methyltransferase activity was measured in extracts of human tumor cells and was partially purified from human placenta. Repair of O6-methylguanine in DNA inactivated the methyltransferase, and treatment of cells with MNNG, which produces this alkylated base in DNA, depleted the cells of active methyltransferase. RNA and protein synthesis were required for restoration of methyltransferase activity, which transiently exceeded the original levels by 50% 48 h after treatment. One species of methyltransferase of Mr = 22 kd was present in human tumor cells and human placenta.

UR - http://www.scopus.com/inward/record.url?scp=48749142060&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=48749142060&partnerID=8YFLogxK

U2 - 10.1016/0167-8817(84)90044-0

DO - 10.1016/0167-8817(84)90044-0

M3 - Article

C2 - 6694657

AN - SCOPUS:48749142060

SN - 0167-8817

VL - 131

SP - 27

EP - 36

JO - Mutation Research DNA Repair Reports

JF - Mutation Research DNA Repair Reports

IS - 1

ER -

O⁶-Methylguanine-DNA methyltransferase in human cells

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this