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Repair of DNA methylphosphotriesters through a metalloactivated cysteine nucleophile.

The Escherichia coli Ada protein repairs methylphosphotriesters in DNA by direct, irreversible methyl transfer to one of its own cysteines. Upon methyl transfer, Ada acquires the ability to bind specific DNA sequences and thereby to induce genes that confer resistance to methylating agents. The amin... Full description

Journal Title: Science (New York N.Y.), August 27, 1993, Vol.261(5125), pp.1164-1167
Main Author: Myers, L C
Other Authors: Terranova, M P , Ferentz, A E , Wagner, G , Verdine, G L
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0036-8075
Link: http://search.proquest.com/docview/75895970/?pq-origsite=primo
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title: Repair of DNA methylphosphotriesters through a metalloactivated cysteine nucleophile.
format: Article
creator:
  • Myers, L C
  • Terranova, M P
  • Ferentz, A E
  • Wagner, G
  • Verdine, G L
subjects:
  • Bacterial Proteins–Chemistry
  • Binding Sites–Genetics
  • Cadmium–Metabolism
  • Cysteine–Metabolism
  • DNA–Metabolism
  • DNA Repair–Chemistry
  • Escherichia Coli Proteins–Metabolism
  • Isotopes–Metabolism
  • Magnetic Resonance Spectroscopy–Metabolism
  • Methylation–Metabolism
  • Mutagenesis, Site-Directed–Metabolism
  • O(6)-Methylguanine-DNA Methyltransferase–Metabolism
  • Protons–Metabolism
  • Transcription Factors–Metabolism
  • Zinc–Metabolism
  • Bacterial Proteins
  • Escherichia Coli Proteins
  • Isotopes
  • Protons
  • Transcription Factors
ispartof: Science (New York, N.Y.), August 27, 1993, Vol.261(5125), pp.1164-1167
description: The Escherichia coli Ada protein repairs methylphosphotriesters in DNA by direct, irreversible methyl transfer to one of its own cysteines. Upon methyl transfer, Ada acquires the ability to bind specific DNA sequences and thereby to induce genes that confer resistance to methylating agents. The amino-terminal domain of Ada, which comprises the methylphosphotriester repair and sequence-specific DNA binding elements, contains a tightly bound zinc ion. Analysis of the zinc binding site by cadmium-113 nuclear magnetic resonance and site-directed mutagenesis revealed that zinc participates in the autocatalytic activation of the active site cysteine and may also function as a conformational switch.
language: eng
source:
identifier: ISSN: 0036-8075
fulltext: fulltext
issn:
  • 00368075
  • 0036-8075
url: Link


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titleRepair of DNA methylphosphotriesters through a metalloactivated cysteine nucleophile.
creatorMyers, L C ; Terranova, M P ; Ferentz, A E ; Wagner, G ; Verdine, G L
contributorMyers, L C (correspondence author) ; Myers, L C (record owner)
ispartofScience (New York, N.Y.), August 27, 1993, Vol.261(5125), pp.1164-1167
identifierISSN: 0036-8075
subjectBacterial Proteins–Chemistry ; Binding Sites–Genetics ; Cadmium–Metabolism ; Cysteine–Metabolism ; DNA–Metabolism ; DNA Repair–Chemistry ; Escherichia Coli Proteins–Metabolism ; Isotopes–Metabolism ; Magnetic Resonance Spectroscopy–Metabolism ; Methylation–Metabolism ; Mutagenesis, Site-Directed–Metabolism ; O(6)-Methylguanine-DNA Methyltransferase–Metabolism ; Protons–Metabolism ; Transcription Factors–Metabolism ; Zinc–Metabolism ; Bacterial Proteins ; Escherichia Coli Proteins ; Isotopes ; Protons ; Transcription Factors
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The Escherichia coli Ada protein repairs methylphosphotriesters in DNA by direct, irreversible methyl transfer to one of its own cysteines. Upon methyl transfer, Ada acquires the ability to bind specific DNA sequences and thereby to induce genes that confer resistance to methylating agents. The amino-terminal domain of Ada, which comprises the methylphosphotriester repair and sequence-specific DNA binding elements, contains a tightly bound zinc ion. Analysis of the zinc binding site by cadmium-113 nuclear magnetic resonance and site-directed mutagenesis revealed that zinc participates in the autocatalytic activation of the active site cysteine and may also function as a conformational switch.

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atitleRepair of DNA methylphosphotriesters through a metalloactivated cysteine nucleophile.
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