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https://www.readbyqxmd.com/read/29789535/coupling-bimolecular-parylation-biosensors-with-genetic-screens-to-identify-parylation-targets
#1
Dragomir B Krastev, Stephen J Pettitt, James Campbell, Feifei Song, Barbara E Tanos, Stoyno S Stoynov, Alan Ashworth, Christopher J Lord
Poly (ADP-ribose)ylation is a dynamic protein modification that regulates multiple cellular processes. Here, we describe a system for identifying and characterizing PARylation events that exploits the ability of a PBZ (PAR-binding zinc finger) protein domain to bind PAR with high-affinity. By linking PBZ domains to bimolecular fluorescent complementation biosensors, we developed fluorescent PAR biosensors that allow the detection of temporal and spatial PARylation events in live cells. Exploiting transposon-mediated recombination, we integrate the PAR biosensor en masse into thousands of protein coding genes in living cells...
May 22, 2018: Nature Communications
https://www.readbyqxmd.com/read/29668892/sumoylation-of-xrcc1-activated-by-poly-adp-ribosyl-ation-regulates-dna-repair
#2
Ling-Yueh Hu, Che-Chang Chang, Yen-Sung Huang, Wen-Cheng Chou, Ying-Mei Lin, Chun-Chen Ho, Wei-Ting Chen, Hsiu-Ming Shih, Chia-Ni Hsiung, Pei-Ei Wu, Chen-Yang Shen
XRCC1 is an essential scaffold protein for base excision repair (BER) and helps to maintain genomic stability. XRCC1 has been indicated as a substrate for small ubiquitin-like modifier modification (SUMOylation); however, how XRCC1 SUMOylation is regulated in cells and how SUMOylated XRCC1 regulates BER activity are not well understood. Here we show that SUMOylation of XRCC1 is regulated in cells under methyl-methanesulfonate (MMS) treatment and facilitates BER. Poly(ADP-ribose) polymerase 1 (PARP1) is activated by MMS immediately and synthesizes poly(ADP-ribose) (PAR), which in turn promotes recruitment of SUMO E3 TOPORS to XRCC1 and facilitates XRCC1 SUMOylation...
April 16, 2018: Human Molecular Genetics
https://www.readbyqxmd.com/read/29664094/analysis-of-poly-adp-ribose-polymerase-1-by-enzyme-initiated-auto-parylation-controlled-aggregation-of-hemin-graphene-nanocomposites
#3
Yong Liu, Xiaolin Xu, Haitang Yang, Ensheng Xu, Shuangshuang Wu, Wei Wei, Jin Chen
Poly(ADP-ribose) polymerase-1 (PARP-1) is a highly conserved nuclear enzyme, which binds tightly to damaged DNA and plays a key role in DNA repair, recombination, proliferation, and genomic stability. However, due to the poor electrochemical and optical activity of PARP-1 and its product PAR, only a few studies on its activity detection method have been reported. Herein, we report a simple and sensitive colorimetric strategy to monitor PARP-1 activity based on enzyme-initiated auto-PARylation-controlled aggregation of hemin-graphene nanocomposites (H-GNs)...
April 17, 2018: Analyst
https://www.readbyqxmd.com/read/29661921/parp1-promotes-the-human-heat-shock-response-by-facilitating-hsf1-binding-to-dna
#4
Mitsuaki Fujimoto, Ryosuke Takii, Arpit Katiyar, Pratibha Srivastava, Akira Nakai
The heat shock response (HSR) is characterized by the rapid and robust induction of heat shock proteins (HSPs), including HSP70, in response to heat shock, and is regulated by heat shock transcription factor 1 (HSF1) in mammalian cells. Poly(ADP-ribose) polymerase 1 (PARP1), which can form a complex with HSF1 through the scaffold protein PARP13, has been suggested to be involved in the HSR. However, its effects on and regulatory mechanisms of the HSR are not well understood. Here, we show that prior to heat shock the HSF1-PARP13-PARP1 complex binds to HSP70 promoter...
April 16, 2018: Molecular and Cellular Biology
https://www.readbyqxmd.com/read/29604130/structural-basis-for-tankyrase-rnf146-interaction-reveals-noncanonical-tankyrase-binding-motifs
#5
Paul A DaRosa, Rachel E Klevit, Wenqing Xu
Poly(ADP-ribosyl)ation (PARylation) catalyzed by the tankyrase enzymes (Tankyrase-1 and -2; a.k.a. PARP-5a and -5b) is involved in mitosis, telomere length regulation, GLUT-4 vesicle transport, and cell growth and differentiation. Together with the E3 ubiquitin ligase RNF146 (a.k.a. Iduna), tankyrases regulate the cellular concentrations of several important proteins including Axin, 3BP2, and angiomotins, which are key regulators of Wnt, Src and hippo signaling, respectively. These substrates of tankyrases are first PARylated and then ubiquitylated by RNF146, which is allosterically activated by binding to PAR polymer...
March 31, 2018: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/29555554/timeless-is-a-novel-estrogen-receptor-co-activator-involved-in-multiple-signaling-pathways-in-mcf-7-cells
#6
Chantal Beatrice Magne Nde, Gloria Casas Gimeno, Maria Docanto, Kevin C Knower, Morag J Young, Jakob Buehn, Edris Sayed, Colin D Clyne
Activation of estrogen receptor α (ERα) stimulates cell division and tumor growth by modulating the expression of ERα target genes. This activation involves the recruitment of specific proteins with activities that are still not fully understood. Timeless, the human homolog of the Drosophila gene involved in circadian rhythm, was previously shown to be a strong predictor of tamoxifen relapse, and is involved in genomic stability and cell cycle control. In this study, we investigated the interplay between Timeless and ERα, and showed that human Timeless is an ERα coactivator...
May 11, 2018: Journal of Molecular Biology
https://www.readbyqxmd.com/read/29549427/analysis-of-hpf1-expression-and-function-in-early-embryonic-development-of-zebrafish
#7
Zhen Zhang, Hongwei Sun, Yu Chen, Tianqi Cao, Zhou Songyang, Junjiu Huang, Yan Huang
About 70% of zebrafish (Danio rerio) genes are orthologues of the human's, which are of great interests, but still largely unknown for their functions. Recently, a report on human histone PARylation factor 1 (HPF1/C4orf27) showed that it is involved in DNA damage response along with poly (ADP-ribose) polymerase 1 (PARP1). However, its function in living organism remains unclear. Given that zebrafish has showed its values in modeling human diseases and physiology, we characterized a zebrafish homolog of human HPF1 by sequence alignment...
March 2018: Development Genes and Evolution
https://www.readbyqxmd.com/read/29535829/poly-adp-ribose-polymerase-1-parp1-modifies-ezh2-and-inhibits-ezh2-histone-methyltransferase-activity-after-dna-damage
#8
Lisa B Caruso, Kayla A Martin, Elisabetta Lauretti, Michael Hulse, Micheal Siciliano, Lena N Lupey-Green, Aaron Abraham, Tomasz Skorski, Italo Tempera
The enzyme Poly(ADP-ribose) polymerase 1 (PARP1) plays a very important role in the DNA damage response, but its role in numerous aspects is not fully understood. We recently showed that in the absence of DNA damage, PARP1 regulates the expression of the chromatin-modifying enzyme EZH2. Work from other groups has shown that EZH2 participates in the DNA damage response. These combined data suggest that EZH2 could be a target of PARP1 in both untreated and genotoxic agent-treated conditions. In this work we tested the hypothesis that, in response to DNA damage, PARP1 regulates EZH2 activity...
February 13, 2018: Oncotarget
https://www.readbyqxmd.com/read/29515234/parp10-suppresses-tumor-metastasis-through-regulation-of-aurora-a-activity
#9
Yahui Zhao, Xiaoding Hu, Li Wei, Dan Song, Juanjuan Wang, Lifang You, Hexige Saiyin, Zhaojie Li, Wenbo Yu, Long Yu, Jin Ding, Jiaxue Wu
ADP-ribosylation, including poly-ADP-ribosylation (PARylation) and mono-ADP-ribosylation (MARylation), is a multifunctional post-translational modification catalyzed by intracellular ADP-ribosyltransferases (ARTDs or PARPs). Although PARylation has been investigated most thoroughly, the function of MARylation is currently largely undefined. Here, we provide evidences that deficiency of PARP10, a mono-ADP-ribosyltransferase, markedly increased the migration and invasion of tumor cells through regulation of epithelial-mesenchymal transition (EMT), and PARP10 inhibited tumor metastasis in vivo, which was dependent on its enzyme activity...
March 8, 2018: Oncogene
https://www.readbyqxmd.com/read/29431122/poly-adp-ribose-polymerase-1-regulates-fibroblast-activation-in-systemic-sclerosis
#10
Yun Zhang, Sebastian Pötter, Chih-Wei Chen, Ruifang Liang, Kolja Gelse, Ingo Ludolph, Raymund E Horch, Oliver Distler, Georg Schett, Jörg H W Distler, Clara Dees
OBJECTIVES: The enzyme poly(ADP-ribose) polymerase-1 (PARP-1) transfers negatively charged ADP-ribose units to target proteins. This modification can have pronounced regulatory effects on target proteins. Recent studies showed that PARP-1 can poly(ADP-ribosyl)ate (PARylate) Smad proteins. However, the role of PARP-1 in the pathogenesis of systemic sclerosis (SSc) has not been investigated. METHODS: The expression of PARP-1 was determined by quantitative PCR and immunohistochemistry...
May 2018: Annals of the Rheumatic Diseases
https://www.readbyqxmd.com/read/29361132/characterization-of-dna-adp-ribosyltransferase-activities-of-parp2-and-parp3-new-insights-into-dna-adp-ribosylation
#11
Gabriella Zarkovic, Ekaterina A Belousova, Ibtissam Talhaoui, Christine Saint-Pierre, Mikhail M Kutuzov, Bakhyt T Matkarimov, Denis Biard, Didier Gasparutto, Olga I Lavrik, Alexander A Ishchenko
Poly(ADP-ribose) polymerases (PARPs) act as DNA break sensors and catalyze the synthesis of polymers of ADP-ribose (PAR) covalently attached to acceptor proteins at DNA damage sites. It has been demonstrated that both mammalian PARP1 and PARP2 PARylate double-strand break termini in DNA oligonucleotide duplexes in vitro. Here, we show that mammalian PARP2 and PARP3 can PARylate and mono(ADP-ribosyl)ate (MARylate), respectively, 5'- and 3'-terminal phosphate residues at double- and single-strand break termini of a DNA molecule containing multiple strand breaks...
March 16, 2018: Nucleic Acids Research
https://www.readbyqxmd.com/read/29327913/proteomic-analysis-of-the-downstream-signaling-network-of-parp1
#12
Yuanli Zhen, Yonghao Yu
Poly-ADP-ribosylation (PARylation) is a protein posttranslational modification (PTM) that is critically involved in many biological processes that are linked to cell stress responses. It is catalyzed by a class of enzymes known as poly-ADP-ribose polymerases (PARPs). In particular, PARP1 is a nuclear protein that is activated upon sensing nicked DNA. Once activated, PARP1 is responsible for the synthesis of a large number of PARylated proteins and initiation of the DNA damage response mechanisms. This observation provided the rationale for developing PARP1 inhibitors for the treatment of human malignancies...
January 30, 2018: Biochemistry
https://www.readbyqxmd.com/read/29250299/oxidative-stress-related-parthanatos-of-circulating-mononuclear-leukocytes-in-heart-failure
#13
Tamás Bárány, Andrea Simon, Gergő Szabó, Rita Benkő, Zsuzsanna Mezei, Levente Molnár, Dávid Becker, Béla Merkely, Endre Zima, Eszter M Horváth
Background: The present study aims to examine the oxidative stress-related activation of poly(ADP-ribose) polymerase (PARP), a cause of parthanatos in circulating mononuclear leukocytes of patients with chronic heart failure (CHF), that was rarely investigated in the human setting yet. Methods: Patients with CHF ( n = 20) and age- and body mass index-matched volunteers ( n = 15) with a normal heart function were enrolled. C-reactive protein, N-terminal probrain-type natriuretic peptide (pro-BNP), plasma total peroxide level (PRX), plasma total antioxidant capacity (TAC), oxidative stress index (OSI), leukocyte lipid peroxidation (4-hydroxynonenal; HNE), protein tyrosine nitration (NT), poly(ADP-ribosyl)ation (PARylation), and apoptosis-inducing factor (AIF) translocation were measured in blood samples of fasting subjects...
2017: Oxidative Medicine and Cellular Longevity
https://www.readbyqxmd.com/read/29234005/proteomic-analyses-identify-arh3-as-a-serine-mono-adp-ribosylhydrolase
#14
Jeannette Abplanalp, Mario Leutert, Emilie Frugier, Kathrin Nowak, Roxane Feurer, Jiro Kato, Hans V A Kistemaker, Dmitri V Filippov, Joel Moss, Amedeo Caflisch, Michael O Hottiger
ADP-ribosylation is a posttranslational modification that exists in monomeric and polymeric forms. Whereas the writers (e.g. ARTD1/PARP1) and erasers (e.g. PARG, ARH3) of poly-ADP-ribosylation (PARylation) are relatively well described, the enzymes involved in mono-ADP-ribosylation (MARylation) have been less well investigated. While erasers for the MARylation of glutamate/aspartate and arginine have been identified, the respective enzymes with specificity for serine were missing. Here we report that, in vitro, ARH3 specifically binds and demodifies proteins and peptides that are MARylated...
December 12, 2017: Nature Communications
https://www.readbyqxmd.com/read/29220652/mechanistic-insights-into-autoinhibition-of-the-oncogenic-chromatin-remodeler-alc1
#15
Laura C Lehmann, Graeme Hewitt, Shintaro Aibara, Alexander Leitner, Emil Marklund, Sarah L Maslen, Varun Maturi, Yang Chen, David van der Spoel, J Mark Skehel, Aristidis Moustakas, Simon J Boulton, Sebastian Deindl
Human ALC1 is an oncogene-encoded chromatin-remodeling enzyme required for DNA repair that possesses a poly(ADP-ribose) (PAR)-binding macro domain. Its engagement with PARylated PARP1 activates ALC1 at sites of DNA damage, but the underlying mechanism remains unclear. Here, we establish a dual role for the macro domain in autoinhibition of ALC1 ATPase activity and coupling to nucleosome mobilization. In the absence of DNA damage, an inactive conformation of the ATPase is maintained by juxtaposition of the macro domain against predominantly the C-terminal ATPase lobe through conserved electrostatic interactions...
December 7, 2017: Molecular Cell
https://www.readbyqxmd.com/read/29216372/the-c-terminal-domain-of-p53-orchestrates-the-interplay-between-non-covalent-and-covalent-poly-adp-ribosyl-ation-of-p53-by-parp1
#16
Arthur Fischbach, Annika Krüger, Stephanie Hampp, Greta Assmann, Lisa Rank, Matthias Hufnagel, Martin T Stöckl, Jan M F Fischer, Sebastian Veith, Pascal Rossatti, Magdalena Ganz, Elisa Ferrando-May, Andrea Hartwig, Karin Hauser, Lisa Wiesmüller, Alexander Bürkle, Aswin Mangerich
The post-translational modification poly(ADP-ribosyl)ation (PARylation) plays key roles in genome maintenance and transcription. Both non-covalent poly(ADP-ribose) binding and covalent PARylation control protein functions, however, it is unknown how the two modes of modification crosstalk mechanistically. Employing the tumor suppressor p53 as a model substrate, this study provides detailed insights into the interplay between non-covalent and covalent PARylation and unravels its functional significance in the regulation of p53...
January 25, 2018: Nucleic Acids Research
https://www.readbyqxmd.com/read/29196784/parp1-protects-from-benzo-a-pyrene-diol-epoxide-induced-replication-stress-and-mutagenicity
#17
Jan M F Fischer, Tabea Zubel, Kirsten Jander, Jelena Fix, Irmela R E A Trussina, Daniel Gebhard, Jörg Bergemann, Alexander Bürkle, Aswin Mangerich
Poly(ADP-ribosyl)ation (PARylation) is a complex and reversible posttranslational modification catalyzed by poly(ADP-ribose)polymerases (PARPs), which orchestrates protein function and subcellular localization. The function of PARP1 in genotoxic stress response upon induction of oxidative DNA lesions and strand breaks is firmly established, but its role in the response to chemical-induced, bulky DNA adducts is understood incompletely. To address the role of PARP1 in the response to bulky DNA adducts, we treated human cancer cells with benzo[a]pyrene 7,8-dihydrodiol-9,10-epoxide (BPDE), which represents the active metabolite of the environmental carcinogen benzo[a]pyrene [B(a)P], in nanomolar to low micromolar concentrations...
December 1, 2017: Archives of Toxicology
https://www.readbyqxmd.com/read/29166620/a-cell-line-specific-atlas-of-parp-mediated-protein-asp-glu-adp-ribosylation-in-breast-cancer
#18
Yuanli Zhen, Yajie Zhang, Yonghao Yu
PARP1 plays a critical role in regulating many biological processes linked to cellular stress responses. Although DNA strand breaks are potent stimuli of PARP1 enzymatic activity, the context-dependent mechanism regulating PARP1 activation and signaling is poorly understood. We performed global characterization of the PARP1-dependent, Asp/Glu-ADP-ribosylated proteome in a panel of cell lines originating from benign breast epithelial cells, as well as common subtypes of breast cancer. From these analyses, we identified 503 specific ADP-ribosylation sites on 322 proteins...
November 21, 2017: Cell Reports
https://www.readbyqxmd.com/read/29121337/parp1-changes-from-three-dimensional-dna-damage-searching-to-one-dimensional-diffusion-after-auto-parylation-or-in-the-presence-of-ape1
#19
Lili Liu, Muwen Kong, Natalie R Gassman, Bret D Freudenthal, Rajendra Prasad, Stephanie Zhen, Simon C Watkins, Samuel H Wilson, Bennett Van Houten
PARP1-dependent poly-ADP-ribosylation (PARylation) participates in the repair of many forms of DNA damage. Here, we used atomic force microscopy (AFM) and single molecule fluorescence microscopy to examine the interactions of PARP1 with common DNA repair intermediates. AFM volume analysis indicates that PARP1 binds to DNA at nicks, abasic (AP) sites, and ends as a monomer. Single molecule DNA tightrope assays were used to follow the real-time dynamic behavior of PARP1 in the absence and presence of AP endonuclease (APE1) on AP DNA damage arrays...
December 15, 2017: Nucleic Acids Research
https://www.readbyqxmd.com/read/29055871/acute-telomerase-components-depletion-triggers-oxidative-stress-as-an-early-event-previous-to-telomeric-shortening
#20
José Santiago Ibáñez-Cabellos, Giselle Pérez-Machado, Marta Seco-Cervera, Ester Berenguer-Pascual, José Luis García-Giménez, Federico V Pallardó
Loss of function of dyskerin (DKC1), NOP10 and TIN2 are responsible for different inheritance patterns of Dyskeratosis congenita (DC; ORPHA1775). They are key components of telomerase (DKC1 and NOP10) and shelterin (TIN2), and play an important role in telomere homeostasis. They participate in several fundamental cellular processes by contributing to Dyskeratosis congenita through mechanisms that are not fully understood. Presence of oxidative stress was postulated to result from telomerase ablation. However, the resulting disturbed redox status can promote telomere attrition by generating a vicious circle, which promotes cellular senescence...
April 2018: Redox Biology
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