Enzymatic removal of O6-methylguanine from DNA by mammalian cell extracts

Research output: Contribution to journalArticle

81 Citations (Scopus)

Abstract

Extracts from various rat tissues were incubated with [3H]methylated DNA or chromatin in order to compare their abilities to catalyze the removal of labeled O6-methylguanine from acid precipitable DNA. Liver extracts had the greatest activity. Kidney extracts had about 35% of the activity in liver and extracts from lung, colon, small intestine and brain were much less active. The enzyme responsible for this reaction does not appear to be an N-glycosidase because no labeled O6-methylguanine could be detected in the supernatant fraction even though more than 50% of this base was lost from the DNA. The released radioactivity was present as methanol which is consistent with the possibility that the reaction may involve a demethylase action on either the DNA substrate or an oligonucleotide derived from it.

Original languageEnglish (US)
Pages (from-to)166-173
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume84
Issue number1
DOIs
StatePublished - Sep 14 1978

Fingerprint

Cell Extracts
Cells
Liver Extracts
DNA
Glycoside Hydrolases
Radioactivity
Oligonucleotides
Small Intestine
Chromatin
Methanol
Rats
Brain
Colon
Tissue
Kidney
Lung
Acids
O-(6)-methylguanine
Substrates
Enzymes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{e87fbc2ef4914ec69d60cbf6a5524a79,
title = "Enzymatic removal of O6-methylguanine from DNA by mammalian cell extracts",
abstract = "Extracts from various rat tissues were incubated with [3H]methylated DNA or chromatin in order to compare their abilities to catalyze the removal of labeled O6-methylguanine from acid precipitable DNA. Liver extracts had the greatest activity. Kidney extracts had about 35{\%} of the activity in liver and extracts from lung, colon, small intestine and brain were much less active. The enzyme responsible for this reaction does not appear to be an N-glycosidase because no labeled O6-methylguanine could be detected in the supernatant fraction even though more than 50{\%} of this base was lost from the DNA. The released radioactivity was present as methanol which is consistent with the possibility that the reaction may involve a demethylase action on either the DNA substrate or an oligonucleotide derived from it.",
author = "Anthony Pegg",
year = "1978",
month = "9",
day = "14",
doi = "10.1016/0006-291X(78)90278-4",
language = "English (US)",
volume = "84",
pages = "166--173",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

Enzymatic removal of O6-methylguanine from DNA by mammalian cell extracts. / Pegg, Anthony.

In: Biochemical and Biophysical Research Communications, Vol. 84, No. 1, 14.09.1978, p. 166-173.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Enzymatic removal of O6-methylguanine from DNA by mammalian cell extracts

AU - Pegg, Anthony

PY - 1978/9/14

Y1 - 1978/9/14

N2 - Extracts from various rat tissues were incubated with [3H]methylated DNA or chromatin in order to compare their abilities to catalyze the removal of labeled O6-methylguanine from acid precipitable DNA. Liver extracts had the greatest activity. Kidney extracts had about 35% of the activity in liver and extracts from lung, colon, small intestine and brain were much less active. The enzyme responsible for this reaction does not appear to be an N-glycosidase because no labeled O6-methylguanine could be detected in the supernatant fraction even though more than 50% of this base was lost from the DNA. The released radioactivity was present as methanol which is consistent with the possibility that the reaction may involve a demethylase action on either the DNA substrate or an oligonucleotide derived from it.

AB - Extracts from various rat tissues were incubated with [3H]methylated DNA or chromatin in order to compare their abilities to catalyze the removal of labeled O6-methylguanine from acid precipitable DNA. Liver extracts had the greatest activity. Kidney extracts had about 35% of the activity in liver and extracts from lung, colon, small intestine and brain were much less active. The enzyme responsible for this reaction does not appear to be an N-glycosidase because no labeled O6-methylguanine could be detected in the supernatant fraction even though more than 50% of this base was lost from the DNA. The released radioactivity was present as methanol which is consistent with the possibility that the reaction may involve a demethylase action on either the DNA substrate or an oligonucleotide derived from it.

UR - http://www.scopus.com/inward/record.url?scp=0018196530&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018196530&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(78)90278-4

DO - 10.1016/0006-291X(78)90278-4

M3 - Article

C2 - 728125

AN - SCOPUS:0018196530

VL - 84

SP - 166

EP - 173

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -