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Science 27 August 1993:
Vol. 261. no. 5125, pp. 1164 - 1167
DOI: 10.1126/science.8395079
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Articles
Science, Vol 261, Issue 5125, 1164-1167
Copyright © 1993 by American Association for the Advancement of Science
Repair of DNA methylphosphotriesters through a metalloactivated cysteine nucleophile
LC Myers,
MP Terranova,
AE Ferentz,
G Wagner,
and
GL Verdine
Program for Higher Degrees in Biophysics, Harvard University, Cambridge, MA 02138.
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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