Abstract:
:The Escherichia coli Ada protein repairs methyl phosphotriesters in DNA by direct, irreversible methyl transfer to one of its own cysteine residues. The methyl-transfer process appears to be autocatalyzed by coordination of the acceptor residue, Cys-69, to a tightly bound zinc ion. Upon methyl transfer, Ada acquires the ability to bind DNA sequence-specifically and thereby to induce genes that confer resistance to methylating agents. The solution structure of an N-terminal 10-kDa fragment of Ada, which retains zinc binding and DNA methyl phosphotriester repair activities, was determined using multidimensional heteronuclear nuclear magnetic resonance techniques. The structure reveals a zinc-binding motif unlike any observed thus far in transcription factors or zinc-containing enzymes and provides insight into the mechanism of metalloactivated DNA repair.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Myers LC,Verdine GL,Wagner Gdoi
10.1021/bi00214a003subject
Has Abstractpub_date
1993-12-28 00:00:00pages
14089-94issue
51eissn
0006-2960issn
1520-4995journal_volume
32pub_type
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