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dc.date.accessioned2020-01-06T20:25:07Z
dc.date.available2020-01-06T20:25:07Z
dc.date.created2019-01-30T12:10:52Z
dc.date.issued2018
dc.identifier.citationGomez, Alvin Bindesbøll, Christian Venkata, Satheesh Grimaldi, Giulia Hutin, David MacPherson, Laura Ahmed, Shaimaa Tamblyn, Laura Cho, Tiffany Nebb, Hilde Irene Moen, Anders Anonsen, Jan Haug Grant, Denis M Matthews, Jason . Characterization of TCDD-inducible poly-ADP-ribose polymerase (TIPARP/ARTD14) catalytic activity. Biochemical Journal. 2018, 475(23), 3827-3846
dc.identifier.urihttp://hdl.handle.net/10852/71906
dc.description.abstractHere, we report the biochemical characterization of the mono-ADP-ribosyltransferase 2,3,7,8-tetrachlorodibenzo-p-dioxin poly-ADP-ribose polymerase (TIPARP/ARTD14/PARP7), which is known to repress aryl hydrocarbon receptor (AHR)-dependent transcription. We found that the nuclear localization of TIPARP was dependent on a short N-terminal sequence and its zinc finger domain. Deletion and in vitro ADP-ribosylation studies identified amino acids 400–657 as the minimum catalytically active region, which retained its ability to mono-ADP-ribosylate AHR. However, the ability of TIPARP to ADP-ribosylate and repress AHR in cells was dependent on both its catalytic activity and zinc finger domain. The catalytic activity of TIPARP was resistant to meta-iodobenzylguanidine but sensitive to iodoacetamide and hydroxylamine, implicating cysteines and acidic side chains as ADP-ribosylated target residues. Mass spectrometry identified multiple ADP-ribosylated peptides in TIPARP and AHR. Electron transfer dissociation analysis of the TIPARP peptide 33ITPLKTCFK41 revealed cysteine 39 as a site for mono-ADP-ribosylation. Mutation of cysteine 39 to alanine resulted in a small, but significant, reduction in TIPARP autoribosylation activity, suggesting that additional amino acid residues are modified, but loss of cysteine 39 did not prevent its ability to repress AHR. Our findings characterize the subcellular localization and mono-ADP-ribosyltransferase activity of TIPARP, identify cysteine as a mono-ADP-ribosylated residue targeted by this enzyme, and confirm the TIPARP-dependent mono-ADP-ribosylation of other protein targets, such as AHR.
dc.languageEN
dc.publisherPortland Press
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.titleCharacterization of TCDD-inducible poly-ADP-ribose polymerase (TIPARP/ARTD14) catalytic activity
dc.typeJournal article
dc.creator.authorGomez, Alvin
dc.creator.authorBindesbøll, Christian
dc.creator.authorVenkata, Satheesh
dc.creator.authorGrimaldi, Giulia
dc.creator.authorHutin, David
dc.creator.authorMacPherson, Laura
dc.creator.authorAhmed, Shaimaa
dc.creator.authorTamblyn, Laura
dc.creator.authorCho, Tiffany
dc.creator.authorNebb, Hilde Irene
dc.creator.authorMoen, Anders
dc.creator.authorAnonsen, Jan Haug
dc.creator.authorGrant, Denis M
dc.creator.authorMatthews, Jason
cristin.unitcode185,51,13,46
cristin.unitnameMolekylær toksikologi
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode2
dc.identifier.cristin1668643
dc.identifier.bibliographiccitationinfo:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biochemical Journal&rft.volume=475&rft.spage=3827&rft.date=2018
dc.identifier.jtitleBiochemical Journal
dc.identifier.volume475
dc.identifier.issue23
dc.identifier.startpage3827
dc.identifier.endpage3846
dc.identifier.doihttps://doi.org/10.1042/BCJ20180347
dc.identifier.urnURN:NBN:no-75026
dc.type.documentTidsskriftartikkel
dc.type.peerreviewedPeer reviewed
dc.source.issn0264-6021
dc.identifier.fulltextFulltext https://www.duo.uio.no/bitstream/handle/10852/71906/4/bcj-2018-0347.pdf
dc.type.versionPublishedVersion


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