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  • 1
    Publication Date: 1996-07-05
    Description: When the Mg2+ ion in the catalytic center of Escherichia coli RNA polymerase (RNAP) is replaced with Fe2+, hydroxyl radicals are generated. In the promoter complex, such radicals cleave template DNA near the transcription start site, whereas the beta' subunit is cleaved at a conserved motif NADFDGD (Asn-Ala-Asp-Phe-Asp-Gly-Asp). Substitution of the three aspartate residues with alanine creates a dominant lethal mutation. The mutant RNAP is catalytically inactive but can bind promoters and form an open complex. The mutant fails to support Fe2+-induced cleavage of DNA or protein. Thus, the NAD-FDGD motif is involved in chelation of the active center Mg2+.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zaychikov, E -- Martin, E -- Denissova, L -- Kozlov, M -- Markovtsov, V -- Kashlev, M -- Heumann, H -- Nikiforov, V -- Goldfarb, A -- Mustaev, A -- New York, N.Y. -- Science. 1996 Jul 5;273(5271):107-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Limnological Institute, Russian Academy of Sciences, Irkutsk, Russia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aspartic Acid/metabolism ; Binding Sites ; DNA/metabolism ; DNA-Directed RNA Polymerases/*chemistry/genetics/*metabolism ; Dithiothreitol/pharmacology ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/*enzymology ; Ferrous Compounds/metabolism ; Hydroxyl Radical ; Magnesium/metabolism ; Molecular Sequence Data ; Mutagenesis ; Promoter Regions, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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