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  1. Article ; Online: Poly-ADP-ribosylation signaling during DNA damage repair.

    Golia, Barbara / Singh, Hari R / Timinszky, Gyula

    Frontiers in bioscience (Landmark edition)

    2015  Volume 20, Issue 3, Page(s) 440–457

    Abstract: Poly-ADP-ribosylation is a post-translational modification generated in high amounts by poly-ADP-ribose polymerases (PARPs) in response to cellular stress, especially genotoxic stimuli. DNA damage-induced PARylation significantly changes local chromatin ... ...

    Abstract Poly-ADP-ribosylation is a post-translational modification generated in high amounts by poly-ADP-ribose polymerases (PARPs) in response to cellular stress, especially genotoxic stimuli. DNA damage-induced PARylation significantly changes local chromatin structure and triggers the accumulation of several DNA damage response (DDR) proteins at the DNA lesions. In this review, we will discuss the regulation of chromatin structure and DNA damage repair machineries by DNA damage-induced poly-ADP-ribosylation.
    MeSH term(s) Chromatin/metabolism ; DNA Damage ; DNA Repair ; Poly Adenosine Diphosphate Ribose/metabolism ; Signal Transduction
    Chemical Substances Chromatin ; Poly Adenosine Diphosphate Ribose (26656-46-2)
    Language English
    Publishing date 2015-01-01
    Publishing country Singapore
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2704569-9
    ISSN 2768-6698 ; 1093-9946
    ISSN (online) 2768-6698
    ISSN 1093-9946
    DOI 10.2741/4318
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Book ; Online ; Thesis: The regulation of the ADP-ribosyl-hydrolase MacroD2 upon DNA damage

    Golia, Barbara [Verfasser] / Ladurner, Andreas [Akademischer Betreuer]

    2017  

    Author's details Barbara Golia ; Betreuer: Andreas Ladurner
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Universitätsbibliothek der Ludwig-Maximilians-Universität
    Publishing place München
    Document type Book ; Online ; Thesis
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  3. Article ; Online: ATM induces MacroD2 nuclear export upon DNA damage.

    Golia, Barbara / Moeller, Giuliana Katharina / Jankevicius, Gytis / Schmidt, Andreas / Hegele, Anna / Preißer, Julia / Tran, Mai Ly / Imhof, Axel / Timinszky, Gyula

    Nucleic acids research

    2017  Volume 45, Issue 1, Page(s) 244–254

    Abstract: ADP-ribosylation is a dynamic post-translation modification that regulates the early phase of various DNA repair pathways by recruiting repair factors to chromatin. ADP-ribosylation levels are defined by the activities of specific transferases and ... ...

    Abstract ADP-ribosylation is a dynamic post-translation modification that regulates the early phase of various DNA repair pathways by recruiting repair factors to chromatin. ADP-ribosylation levels are defined by the activities of specific transferases and hydrolases. However, except for the transferase PARP1/ARDT1 little is known about regulation of these enzymes. We found that MacroD2, a mono-ADP-ribosylhydrolase, is exported from the nucleus upon DNA damage, and that this nuclear export is induced by ATM activity. We show that the export is dependent on the phosphorylation of two SQ/TQ motifs, suggesting a novel direct interaction between ATM and ADP-ribosylation. Lastly, we show that MacroD2 nuclear export temporally restricts its recruitment to DNA lesions, which may decrease the net ADP-ribosylhydrolase activity at the site of DNA damage. Together, our results identify a novel feedback regulation between two crucial DNA damage-induced signaling pathways: ADP-ribosylation and ATM activation.
    MeSH term(s) Active Transport, Cell Nucleus ; Adenosine Diphosphate/metabolism ; Amino Acid Motifs ; Ataxia Telangiectasia Mutated Proteins/genetics ; Ataxia Telangiectasia Mutated Proteins/metabolism ; Cell Line, Tumor ; Cell Nucleus/metabolism ; DNA Damage ; DNA Repair Enzymes/genetics ; DNA Repair Enzymes/metabolism ; Feedback, Physiological ; HeLa Cells ; Humans ; Hydrolases/genetics ; Hydrolases/metabolism ; Osteoblasts ; Phosphorylation ; Poly(ADP-ribose) Polymerases/genetics ; Poly(ADP-ribose) Polymerases/metabolism ; Protein Processing, Post-Translational ; Signal Transduction
    Chemical Substances MACROD2 protein, human ; Adenosine Diphosphate (61D2G4IYVH) ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30) ; ATM protein, human (EC 2.7.11.1) ; Ataxia Telangiectasia Mutated Proteins (EC 2.7.11.1) ; Hydrolases (EC 3.-) ; DNA Repair Enzymes (EC 6.5.1.-)
    Language English
    Publishing date 2017-01-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkw904
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1067: Show issues Location:
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  4. Article ; Online: A family of macrodomain proteins reverses cellular mono-ADP-ribosylation.

    Jankevicius, Gytis / Hassler, Markus / Golia, Barbara / Rybin, Vladimir / Zacharias, Martin / Timinszky, Gyula / Ladurner, Andreas G

    Nature structural & molecular biology

    2013  Volume 20, Issue 4, Page(s) 508–514

    Abstract: ADP-ribosylation is a reversible post-translational modification with wide-ranging biological functions in all kingdoms of life. A variety of enzymes use NAD(+) to transfer either single or multiple ADP-ribose (ADPr) moieties onto distinct amino acid ... ...

    Abstract ADP-ribosylation is a reversible post-translational modification with wide-ranging biological functions in all kingdoms of life. A variety of enzymes use NAD(+) to transfer either single or multiple ADP-ribose (ADPr) moieties onto distinct amino acid substrates, often in response to DNA damage or other stresses. Poly-ADPr-glycohydrolase readily reverses poly-ADP-ribosylation induced by the DNA-damage sensor PARP1 and other enzymes, but it does not remove the most proximal ADPr linked to the target amino acid. Searches for enzymes capable of fully reversing cellular mono-ADP-ribosylation back to the unmodified state have proved elusive, which leaves a gap in the understanding of this modification. Here, we identify a family of macrodomain enzymes present in viruses, yeast and animals that reverse cellular ADP-ribosylation by acting on mono-ADP-ribosylated substrates. Our discoveries establish the complete reversibility of PARP-catalyzed cellular ADP-ribosylation as a regulatory modification.
    MeSH term(s) Adenosine Diphosphate Ribose/metabolism ; Amino Acid Sequence ; Biocatalysis ; Models, Molecular ; Molecular Sequence Data ; N-Glycosyl Hydrolases/chemistry ; N-Glycosyl Hydrolases/metabolism ; Protein Binding ; Protein Processing, Post-Translational ; Proteins/metabolism ; Sequence Homology, Amino Acid
    Chemical Substances Proteins ; Adenosine Diphosphate Ribose (20762-30-5) ; N-Glycosyl Hydrolases (EC 3.2.2.-) ; ADP-ribosylarginine hydrolase (EC 3.2.2.19)
    Keywords covid19
    Language English
    Publishing date 2013-03-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/nsmb.2523
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4101: Show issues Location:
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    Zs.MG 56: Show issues

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  5. Article ; Online: Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease.

    Sharifi, Reza / Morra, Rosa / Appel, C Denise / Tallis, Michael / Chioza, Barry / Jankevicius, Gytis / Simpson, Michael A / Matic, Ivan / Ozkan, Ege / Golia, Barbara / Schellenberg, Matthew J / Weston, Ria / Williams, Jason G / Rossi, Marianna N / Galehdari, Hamid / Krahn, Juno / Wan, Alexander / Trembath, Richard C / Crosby, Andrew H /
    Ahel, Dragana / Hay, Ron / Ladurner, Andreas G / Timinszky, Gyula / Williams, R Scott / Ahel, Ivan

    The EMBO journal

    2013  Volume 32, Issue 9, Page(s) 1225–1237

    Abstract: Adenosine diphosphate (ADP)-ribosylation is a post-translational protein modification implicated in the regulation of a range of cellular processes. A family of proteins that catalyse ADP-ribosylation reactions are the poly(ADP-ribose) (PAR) polymerases ( ...

    Abstract Adenosine diphosphate (ADP)-ribosylation is a post-translational protein modification implicated in the regulation of a range of cellular processes. A family of proteins that catalyse ADP-ribosylation reactions are the poly(ADP-ribose) (PAR) polymerases (PARPs). PARPs covalently attach an ADP-ribose nucleotide to target proteins and some PARP family members can subsequently add additional ADP-ribose units to generate a PAR chain. The hydrolysis of PAR chains is catalysed by PAR glycohydrolase (PARG). PARG is unable to cleave the mono(ADP-ribose) unit directly linked to the protein and although the enzymatic activity that catalyses this reaction has been detected in mammalian cell extracts, the protein(s) responsible remain unknown. Here, we report the homozygous mutation of the c6orf130 gene in patients with severe neurodegeneration, and identify C6orf130 as a PARP-interacting protein that removes mono(ADP-ribosyl)ation on glutamate amino acid residues in PARP-modified proteins. X-ray structures and biochemical analysis of C6orf130 suggest a mechanism of catalytic reversal involving a transient C6orf130 lysyl-(ADP-ribose) intermediate. Furthermore, depletion of C6orf130 protein in cells leads to proliferation and DNA repair defects. Collectively, our data suggest that C6orf130 enzymatic activity has a role in the turnover and recycling of protein ADP-ribosylation, and we have implicated the importance of this protein in supporting normal cellular function in humans.
    MeSH term(s) Amino Acid Sequence ; Base Sequence ; Cells, Cultured ; Child ; Child, Preschool ; Family ; Female ; Glycoside Hydrolases/genetics ; Glycoside Hydrolases/physiology ; HEK293 Cells ; HeLa Cells ; Humans ; Male ; Models, Molecular ; Molecular Sequence Data ; Neurodegenerative Diseases/enzymology ; Neurodegenerative Diseases/genetics ; Pedigree ; Poly Adenosine Diphosphate Ribose/genetics ; Poly Adenosine Diphosphate Ribose/physiology ; Protein Processing, Post-Translational/genetics ; Sequence Homology, Amino Acid ; Thiolester Hydrolases/genetics ; Thiolester Hydrolases/physiology
    Chemical Substances Poly Adenosine Diphosphate Ribose (26656-46-2) ; OARD1 protein, human (EC 3.1.2.-) ; Thiolester Hydrolases (EC 3.1.2.-) ; Glycoside Hydrolases (EC 3.2.1.-)
    Language English
    Publishing date 2013-03-12
    Publishing country England
    Document type Case Reports ; Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/emboj.2013.51
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1808: Show issues Location:
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    Zs.MG 100: Show issues

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