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    Flipping of alkylated DNA damage bridges base and nucleotide excision repair.

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    Authors
    Tubbs, Julie L
    Latypov, Vitaly F
    Kanugula, Sreenivas
    Butt, Amna
    Melikishvili, Manana
    Kraehenbuehl, Rolf
    Fleck, Oliver
    Marriott, Andrew S
    Watson, Amanda J
    Verbeek, Barbara
    McGown, Gail
    Thorncroft, Mary R
    Santibanez-Koref, Mauro F
    Millington, Christopher
    Arvai, Andrew S
    Kroeger, Matthew D
    Peterson, Lisa A
    Williams, David M
    Fried, Mike
    Margison, Geoffrey P
    Pegg, Anthony E
    Tainer, John A
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    Affiliation
    Skaggs Institute for Chemical Biology and Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
    Issue Date
    2009-06-11
    
    Metadata
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    Abstract
    Alkyltransferase-like proteins (ATLs) share functional motifs with the cancer chemotherapy target O(6)-alkylguanine-DNA alkyltransferase (AGT) and paradoxically protect cells from the biological effects of DNA alkylation damage, despite lacking the reactive cysteine and alkyltransferase activity of AGT. Here we determine Schizosaccharomyces pombe ATL structures without and with damaged DNA containing the endogenous lesion O(6)-methylguanine or cigarette-smoke-derived O(6)-4-(3-pyridyl)-4-oxobutylguanine. These results reveal non-enzymatic DNA nucleotide flipping plus increased DNA distortion and binding pocket size compared to AGT. Our analysis of lesion-binding site conservation identifies new ATLs in sea anemone and ancestral archaea, indicating that ATL interactions are ancestral to present-day repair pathways in all domains of life. Genetic connections to mammalian XPG (also known as ERCC5) and ERCC1 in S. pombe homologues Rad13 and Swi10 and biochemical interactions with Escherichia coli UvrA and UvrC combined with structural results reveal that ATLs sculpt alkylated DNA to create a genetic and structural intersection of base damage processing with nucleotide excision repair.
    Citation
    Flipping of alkylated DNA damage bridges base and nucleotide excision repair. 2009, 459 (7248):808-13 Nature
    Journal
    Nature
    URI
    http://hdl.handle.net/10541/85244
    DOI
    10.1038/nature08076
    PubMed ID
    19516334
    Type
    Article
    Language
    en
    ISSN
    1476-4687
    ae974a485f413a2113503eed53cd6c53
    10.1038/nature08076
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research
    Carcinogenesis Group
    Medical Oncology

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