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Journal articles on the topic 'Mono-ADP-ribose'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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1

Haikarainen, Teemu, Mirko M. Maksimainen, Ezeogo Obaji, and Lari Lehtiö. "Development of an Inhibitor Screening Assay for Mono-ADP-Ribosyl Hydrolyzing Macrodomains Using AlphaScreen Technology." SLAS DISCOVERY: Advancing the Science of Drug Discovery 23, no. 3 (2017): 255–63. http://dx.doi.org/10.1177/2472555217737006.

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Protein mono-ADP-ribosylation is a posttranslational modification involved in the regulation of several cellular signaling pathways. Cellular ADP-ribosylation is regulated by ADP-ribose hydrolases via a hydrolysis of the protein-linked ADP-ribose. Most of the ADP-ribose hydrolases share a macrodomain fold. Macrodomains have been linked to several diseases, such as cancer, but their cellular roles are mostly unknown. Currently, there are no inhibitors available targeting the mono-ADP-ribose hydrolyzing macrodomains. We have developed a robust AlphaScreen assay for the screening of inhibitors ag

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2

Hassa, Paul O., Sandra S. Haenni, Michael Elser, and Michael O. Hottiger. "Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?" Microbiology and Molecular Biology Reviews 70, no. 3 (2006): 789–829. http://dx.doi.org/10.1128/mmbr.00040-05.

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SUMMARY Since poly-ADP ribose was discovered over 40 years ago, there has been significant progress in research into the biology of mono- and poly-ADP-ribosylation reactions. During the last decade, it became clear that ADP-ribosylation reactions play important roles in a wide range of physiological and pathophysiological processes, including inter- and intracellular signaling, transcriptional regulation, DNA repair pathways and maintenance of genomic stability, telomere dynamics, cell differentiation and proliferation, and necrosis and apoptosis. ADP-ribosylation reactions are phylogeneticall

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3

Kasson, Samuel, Nuwani Dharmapriya, and In-Kwon Kim. "Selective monitoring of the protein-free ADP-ribose released by ADP-ribosylation reversal enzymes." PLOS ONE 16, no. 6 (2021): e0254022. http://dx.doi.org/10.1371/journal.pone.0254022.

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ADP-ribosylation is a key post-translational modification that regulates a wide variety of cellular stress responses. The ADP-ribosylation cycle is maintained by writers and erasers. For example, poly(ADP-ribosyl)ation cycles consist of two predominant enzymes, poly(ADP-ribose) polymerases (PARPs) and poly(ADP-ribose) glycohydrolase (PARG). However, historically, mechanisms of erasers of ADP-ribosylations have been understudied, primarily due to the lack of quantitative tools to selectively monitor specific activities of different ADP-ribosylation reversal enzymes. Here, we developed a new NUD

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4

Liu, Qiang, Gijsbert A. van der Marel, and Dmitri V. Filippov. "Chemical ADP-ribosylation: mono-ADPr-peptides and oligo-ADP-ribose." Organic & Biomolecular Chemistry 17, no. 22 (2019): 5460–74. http://dx.doi.org/10.1039/c9ob00501c.

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5

Mendoza-Alvarez, Hilda, and Rafael Alvarez-Gonzalez. "Biochemical Characterization of Mono(ADP-ribosyl)ated Poly(ADP-ribose) Polymerase†." Biochemistry 38, no. 13 (1999): 3948–53. http://dx.doi.org/10.1021/bi982148p.

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6

Boulikas, Teni, and Guy G. Poirier. "Resistance of ADP-ribosylated histones and HMG proteins to proteases." Biochemistry and Cell Biology 70, no. 10-11 (1992): 1258–67. http://dx.doi.org/10.1139/o92-172.

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Calf thymus histones (individually isolated or mixtures) and high mobility group proteins were ADP-ribosylated in vitro using [32P]NAD+ and immobilized purified poly(ADP-ribose) polymerase. The modified histones were then subjected to V8 protease or α-chymotrypsin digestion and the resulting peptides were separated by electrophoresis on acetic acid – urea – Triton gels. It was found that in vitro ADP-ribosylated histones were much more resistant to proteases than unmodified histones. A similar approach was applied to histones modified by the endogenous poly(ADP-ribose) polymerase in permeabili

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7

DONNELLY, Louise E., Nigel B. RENDELL, Stephen MURRAY, et al. "Arginine-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes." Biochemical Journal 315, no. 2 (1996): 635–41. http://dx.doi.org/10.1042/bj3150635.

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An Arg-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes (PMNs) was confirmed by the use of diethylamino(benzylidineamino)guanidine (DEA-BAG) as an ADP-ribose acceptor. Two separate HPLC systems were used to separate ADP-ribosyl-DEA-BAG from reaction mixtures, and its presence was confirmed by electrospray mass spectrometry. ADP-ribosyl-DEA-BAG was produced in the presence of PMNs, but not in their absence. Incubation of DEA-BAG with ADP-ribose (0.1–10 mM) did not yield ADP-ribosyl-DEA-BAG, which indicates that ADP-ribosyl-DEA-BAG fo

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8

Ishiwata-Endo, Hiroko, Jiro Kato, Linda A. Stevens, and Joel Moss. "ARH1 in Health and Disease." Cancers 12, no. 2 (2020): 479. http://dx.doi.org/10.3390/cancers12020479.

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Arginine-specific mono-adenosine diphosphate (ADP)-ribosylation is a nicotinamide adenine dinucleotide (NAD)+-dependent, reversible post-translational modification involving the transfer of an ADP-ribose from NAD+ by bacterial toxins and eukaryotic ADP-ribosyltransferases (ARTs) to arginine on an acceptor protein or peptide. ADP-ribosylarginine hydrolase 1 (ARH1) catalyzes the cleavage of the ADP-ribose-arginine bond, regenerating (arginine)protein. Arginine-specific mono-ADP-ribosylation catalyzed by bacterial toxins was first identified as a mechanism of disease pathogenesis. Cholera toxin A

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9

McPherson, Robert Lyle, Rachy Abraham, Easwaran Sreekumar, et al. "ADP-ribosylhydrolase activity of Chikungunya virus macrodomain is critical for virus replication and virulence." Proceedings of the National Academy of Sciences 114, no. 7 (2017): 1666–71. http://dx.doi.org/10.1073/pnas.1621485114.

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Chikungunya virus (CHIKV), an Old World alphavirus, is transmitted to humans by infected mosquitoes and causes acute rash and arthritis, occasionally complicated by neurologic disease and chronic arthritis. One determinant of alphavirus virulence is nonstructural protein 3 (nsP3) that contains a highly conserved MacroD-type macrodomain at the N terminus, but the roles of nsP3 and the macrodomain in virulence have not been defined. Macrodomain is a conserved protein fold found in several plus-strand RNA viruses that binds to the small molecule ADP-ribose. Prototype MacroD-type macrodomains also

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10

Gomez, Alvin, Christian Bindesbøll, Somisetty V. Satheesh, et al. "Characterization of TCDD-inducible poly-ADP-ribose polymerase (TIPARP/ARTD14) catalytic activity." Biochemical Journal 475, no. 23 (2018): 3827–46. http://dx.doi.org/10.1042/bcj20180347.

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Here, 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

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11

Banasik, M., H. Komura, M. Shimoyama, and K. Ueda. "Specific inhibitors of poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferase." Journal of Biological Chemistry 267, no. 3 (1992): 1569–75. http://dx.doi.org/10.1016/s0021-9258(18)45983-2.

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12

Martinez, Marcos, S. Russ Price, Joel Moss, and Rafael Alvarez-Gonzalez. "Mono(ADP-ribosyl)ation of poly(ADP-ribose)polymerase by cholera toxin." Biochemical and Biophysical Research Communications 181, no. 3 (1991): 1412–18. http://dx.doi.org/10.1016/0006-291x(91)92096-3.

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13

Li, Changqing, Yannick Debing, Gytis Jankevicius, et al. "Viral Macro Domains Reverse Protein ADP-Ribosylation." Journal of Virology 90, no. 19 (2016): 8478–86. http://dx.doi.org/10.1128/jvi.00705-16.

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ABSTRACTADP-ribosylation is a posttranslational protein modification in which ADP-ribose is transferred from NAD+to specific acceptors to regulate a wide variety of cellular processes. The macro domain is an ancient and highly evolutionarily conserved protein domain widely distributed throughout all kingdoms of life, including viruses. The human TARG1/C6orf130, MacroD1, and MacroD2 proteins can reverse ADP-ribosylation by acting on ADP-ribosylated substrates through the hydrolytic activity of their macro domains. Here, we report that the macro domain from hepatitis E virus (HEV) serves as an A

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14

Bindesbøll, Christian, Susanna Tan, Debbie Bott, et al. "TCDD-inducible poly-ADP-ribose polymerase (TIPARP/PARP7) mono-ADP-ribosylates and co-activates liver X receptors." Biochemical Journal 473, no. 7 (2016): 899–910. http://dx.doi.org/10.1042/bj20151077.

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2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD)-inducible poly-ADP-ribose polymerase (TIPARP), mono-ADP-ribosylated and positively regulated liver X receptor α (LXRα) and LXRβ activity. The ability of TIPARP to increase LXR activity was also reversed by macrodomain 1 (MACROD1), suggesting that reversible ADP-ribosylation regulates LXR activity.

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15

Bauer, Pal I., Alaeddin Hakam, and Ernest Kun. "Mechanisms of poly(ADP-ribose) polymerase catalysis; mono-ADP-ribosylation of poly(ADP-ribose) polymerase at nanomolar concentrations of NAD." FEBS Letters 195, no. 1-2 (1986): 331–38. http://dx.doi.org/10.1016/0014-5793(86)80188-0.

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16

Beijer, Danique, Thomas Agnew, Johannes Gregor Matthias Rack, et al. "Biallelic ADPRHL2 mutations in complex neuropathy affect ADP ribosylation and DNA damage response." Life Science Alliance 4, no. 11 (2021): e202101057. http://dx.doi.org/10.26508/lsa.202101057.

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ADP ribosylation is a reversible posttranslational modification mediated by poly(ADP-ribose)transferases (e.g., PARP1) and (ADP-ribosyl)hydrolases (e.g., ARH3 and PARG), ensuring synthesis and removal of mono-ADP-ribose or poly-ADP-ribose chains on protein substrates. Dysregulation of ADP ribosylation signaling has been associated with several neurodegenerative diseases, including Parkinson’s disease, amyotrophic lateral sclerosis, and Huntington’s disease. Recessive ADPRHL2/ARH3 mutations are described to cause a stress-induced epileptic ataxia syndrome with developmental delay and axonal neu

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17

Wallrodt, Sarah, Edward L. Simpson, and Andreas Marx. "Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NAD+ analogues." Beilstein Journal of Organic Chemistry 13 (March 10, 2017): 495–501. http://dx.doi.org/10.3762/bjoc.13.49.

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ADP-ribosyl transferases with diphtheria toxin homology (ARTDs) catalyse the covalent addition of ADP-ribose onto different acceptors forming mono- or poly(ADP-ribos)ylated proteins. Out of the 18 members identified, only four are known to synthesise the complex poly(ADP-ribose) biopolymer. The investigation of this posttranslational modification is important due to its involvement in cancer and other diseases. Lately, metabolic labelling approaches comprising different reporter-modified NAD+ building blocks have stimulated and enriched proteomic studies and imaging applications of ADP-ribosyl

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18

Kincaid, John WR, and Nathan A. Berger. "NAD metabolism in aging and cancer." Experimental Biology and Medicine 245, no. 17 (2020): 1594–614. http://dx.doi.org/10.1177/1535370220929287.

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NAD+ and its derivatives NADH, NADP+, and NADPH are essential cofactors in redox reactions and electron transport pathways. NAD serves also as substrate for an extensive series of regulatory enzymes including cyclic ADP-ribose hydrolases, mono(ADP-ribosyl)transferases, poly(ADP-ribose) polymerases, and sirtuin deacetylases which are O-acetyl-ADP-ribosyltransferases. As a result of the numerous and diverse enzymes that utilize NAD as well as depend on its synthesis and concentration, significant interest has developed in its role in a variety of physiologic and pathologic processes, and therape

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19

JONES, Ellene M., and Andrew BAIRD. "Cell-surface ADP-ribosylation of fibroblast growth factor-2 by an arginine-specific ADP-ribosyltransferase." Biochemical Journal 323, no. 1 (1997): 173–77. http://dx.doi.org/10.1042/bj3230173.

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Basic fibroblast growth factor (FGF-2) appeared to be ADP-ribosylated on the surface of adult bovine aortic arch endothelial and human hepatoma cells. Further characterization of this reaction with cells expressing an arginine-specific, glycosylphosphatidylinositol-anchored, mono-ADP-ribosyltransferase demonstrated that FGF-2 is ADP-ribosylated on arginine. Incubation of transformed cells with FGF-2 and [adenylate-32P]nicotinamide-adenine dinucleotide (NAD) resulted in the rapid incorporation of [32P]ADP-ribose into FGF-2 in a time-and concentration-dependent manner, with labelling averaging 3

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20

Wazir, Sarah, Mirko M. Maksimainen, and Lari Lehtiö. "Multiple crystal forms of human MacroD2." Acta Crystallographica Section F Structural Biology Communications 76, no. 10 (2020): 477–82. http://dx.doi.org/10.1107/s2053230x20011309.

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MacroD2 is one of the three human macrodomain proteins characterized by their protein-linked mono-ADP-ribosyl-hydrolyzing activity. MacroD2 is a single-domain protein that contains a deep ADP-ribose-binding groove. In this study, new crystallization conditions for MacroD2 were found and three crystal structures of human MacroD2 in the apo state were solved in space groups P41212, P43212 and P43, and refined at 1.75, 1.90 and 1.70 Å resolution, respectively. Structural comparison of the apo crystal structures with the previously reported crystal structure of MacroD2 in complex with ADP-ribose r

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21

Wazir, Sarah, Mirko M. Maksimainen, Heli I. Alanen, Albert Galera-Prat, and Lari Lehtiö. "Activity-Based Screening Assay for Mono-ADP-Ribosylhydrolases." SLAS DISCOVERY: Advancing the Science of Drug Discovery 26, no. 1 (2020): 67–76. http://dx.doi.org/10.1177/2472555220928911.

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ADP-ribosylation is a post-translational modification involved in the regulation of many vital cellular processes. This posttranslational modification is carried out by ADP-ribosyltransferases converting β-NAD+ into nicotinamide and a protein-linked ADP-ribosyl group or a chain of PAR. The reverse reaction, release of ADP-ribose from the acceptor molecule, is catalyzed by ADP-ribosylhydrolases. Several hydrolases contain a macrodomain fold, and activities of human macrodomain protein modules vary from reading or erasing mono- and poly-ADP-ribosylation. Macrodomains have been linked to diseases

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22

Ekblad, Torun, Patricia Verheugd, Anders E. Lindgren, Tomas Nyman, Mikael Elofsson, and Herwig Schüler. "Identification of Poly(ADP-Ribose) Polymerase Macrodomain Inhibitors Using an AlphaScreen Protocol." SLAS DISCOVERY: Advancing the Science of Drug Discovery 23, no. 4 (2018): 353–62. http://dx.doi.org/10.1177/2472555217750870.

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Macrodomains recognize intracellular adenosine diphosphate (ADP)-ribosylation resulting in either removal of the modification or a protein interaction event. Research into compounds that modulate macrodomain functions could make important contributions. We investigated the interactions of all seven individual macrodomains of the human poly(ADP-ribose) polymerase (PARP) family members PARP9, PARP14, and PARP15 with five mono-ADP-ribosylated (automodified) ADP-ribosyltransferase domains using an AlphaScreen assay. Several mono-ADP-ribosylation-dependent interactions were identified, and they wer

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GASMI, Lakhdar, Jared L. CARTWRIGHT, and Alexander G. MCLENNAN. "Cloning, expression and characterization of YSA1H, a human adenosine 5′-diphosphosugar pyrophosphatase possessing a MutT motif." Biochemical Journal 344, no. 2 (1999): 331–37. http://dx.doi.org/10.1042/bj3440331.

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The human homologue of the Saccharomyces cerevisiae YSA1 protein, YSA1H, has been expressed as a thioredoxin fusion protein in Escherichia coli. It is an ADP-sugar pyrophosphatase with similar activities towards ADP-ribose and ADP-mannose. Its activities with ADP-glucose and diadenosine diphosphate were 56% and 20% of that with ADP-ribose respectively, whereas its activity towards other nucleoside 5′-diphosphosugars was typically 2-10%. cADP-ribose was not a substrate. The products of ADP-ribose hydrolysis were AMP and ribose 5-phosphate. Km and kcat values with ADP-ribose were 60 μM and 5.5 s

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Morrison, Alan R., Joel Moss, Linda A. Stevens, et al. "ART2, a T Cell Surface Mono-ADP-ribosyltransferase, Generates Extracellular Poly(ADP-ribose)." Journal of Biological Chemistry 281, no. 44 (2006): 33363–72. http://dx.doi.org/10.1074/jbc.m607259200.

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Balducci, Enrico, Alessio Bonucci, Monica Picchianti, Rebecca Pogni та Eleonora Talluri. "Structural and Functional Consequences Induced by Post-Translational Modifications in α-Defensins". International Journal of Peptides 2011 (28 серпня 2011): 1–7. http://dx.doi.org/10.1155/2011/594723.

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HNP-1 is an antimicrobial peptide that undergoes proteolytic cleavage to become a mature peptide. This process represents the mechanism commonly used by the cells to obtain a fully active antimicrobial peptide. In addition, it has been recently described that HNP-1 is recognized as substrate by the arginine-specific ADP-ribosyltransferase-1. Arginine-specific mono-ADP-ribosylation is an enzyme-catalyzed post-translational modification in which NAD+ serves as donor of the ADP-ribose moiety, which is transferred to the guanidino group of arginines in target proteins. While the arginine carries o

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Wigle, Tim J., W. David Church, Christina R. Majer, et al. "Forced Self-Modification Assays as a Strategy to Screen MonoPARP Enzymes." SLAS DISCOVERY: Advancing the Science of Drug Discovery 25, no. 3 (2019): 241–52. http://dx.doi.org/10.1177/2472555219883623.

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Mono(ADP-ribosylation) (MARylation) and poly(ADP-ribosylation) (PARylation) are posttranslational modifications found on multiple amino acids. There are 12 enzymatically active mono(ADP-ribose) polymerase (monoPARP) enzymes and 4 enzymatically active poly(ADP-ribose) polymerase (polyPARP) enzymes that use nicotinamide adenine dinucleotide (NAD+) as the ADP-ribose donating substrate to generate these modifications. While there are approved drugs and clinical trials ongoing for the enzymes that perform PARylation, MARylation is gaining recognition for its role in immune function, inflammation, a

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Poltronieri, Palmiro, Angela Celetti, and Luca Palazzo. "Mono(ADP-ribosyl)ation Enzymes and NAD+ Metabolism: A Focus on Diseases and Therapeutic Perspectives." Cells 10, no. 1 (2021): 128. http://dx.doi.org/10.3390/cells10010128.

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Mono(ADP-ribose) transferases and mono(ADP-ribosyl)ating sirtuins use NAD+ to perform the mono(ADP-ribosyl)ation, a simple form of post-translational modification of proteins and, in some cases, of nucleic acids. The availability of NAD+ is a limiting step and an essential requisite for NAD+ consuming enzymes. The synthesis and degradation of NAD+, as well as the transport of its key intermediates among cell compartments, play a vital role in the maintenance of optimal NAD+ levels, which are essential for the regulation of NAD+-utilizing enzymes. In this review, we provide an overview of the c

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Poltronieri, Palmiro, Angela Celetti, and Luca Palazzo. "Mono(ADP-ribosyl)ation Enzymes and NAD+ Metabolism: A Focus on Diseases and Therapeutic Perspectives." Cells 10, no. 1 (2021): 128. http://dx.doi.org/10.3390/cells10010128.

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Mono(ADP-ribose) transferases and mono(ADP-ribosyl)ating sirtuins use NAD+ to perform the mono(ADP-ribosyl)ation, a simple form of post-translational modification of proteins and, in some cases, of nucleic acids. The availability of NAD+ is a limiting step and an essential requisite for NAD+ consuming enzymes. The synthesis and degradation of NAD+, as well as the transport of its key intermediates among cell compartments, play a vital role in the maintenance of optimal NAD+ levels, which are essential for the regulation of NAD+-utilizing enzymes. In this review, we provide an overview of the c

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Moyle, Peter M., and Tom W. Muir. "Method for the Synthesis of Mono-ADP-ribose Conjugated Peptides." Journal of the American Chemical Society 132, no. 45 (2010): 15878–80. http://dx.doi.org/10.1021/ja1064312.

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30

Turgeon, Zachari, René Jørgensen, Danielle Visschedyk, et al. "Newly Discovered and Characterized Antivirulence Compounds Inhibit Bacterial Mono-ADP-Ribosyltransferase Toxins." Antimicrobial Agents and Chemotherapy 55, no. 3 (2010): 983–91. http://dx.doi.org/10.1128/aac.01164-10.

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ABSTRACTThe mono-ADP-ribosyltransferase toxins are bacterial virulence factors that contribute to many disease states in plants, animals, and humans. These toxins function as enzymes that target various host proteins and covalently attach an ADP-ribose moiety that alters target protein function. We tested compounds from a virtual screen of commercially available compounds combined with a directed poly(ADP-ribose) polymerase (PARP) inhibitor library and found several compounds that bind tightly and inhibit toxins fromPseudomonas aeruginosaandVibrio cholerae. The most efficacious compounds compl

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Smith, Kelly P., Robert C. Benjamin, Joel Moss, and Myron K. Jacobson. "Identification of enzymatic activities which process protein bound mono(ADP-ribose)." Biochemical and Biophysical Research Communications 126, no. 1 (1985): 136–42. http://dx.doi.org/10.1016/0006-291x(85)90582-0.

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Rasmussen, Marit, Susanna Tan, Venkata S. Somisetty та ін. "PARP7 and Mono-ADP-Ribosylation Negatively Regulate Estrogen Receptor α Signaling in Human Breast Cancer Cells". Cells 10, № 3 (2021): 623. http://dx.doi.org/10.3390/cells10030623.

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ADP-ribosylation is a post-translational protein modification catalyzed by a family of proteins known as poly-ADP-ribose polymerases. PARP7 (TIPARP; ARTD14) is a mono-ADP-ribosyltransferase involved in several cellular processes, including responses to hypoxia, innate immunity and regulation of nuclear receptors. Since previous studies suggested that PARP7 was regulated by 17β-estradiol, we investigated whether PARP7 regulates estrogen receptor α signaling. We confirmed the 17β-estradiol-dependent increases of PARP7 mRNA and protein levels in MCF-7 cells, and observed recruitment of estrogen r

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YATES, Susan P., Patricia L. TAYLOR, René JØRGENSEN, et al. "Structure–function analysis of water-soluble inhibitors of the catalytic domain of exotoxin A from Pseudomonas aeruginosa." Biochemical Journal 385, no. 3 (2005): 667–75. http://dx.doi.org/10.1042/bj20041480.

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The mono-ADPRT (mono-ADP-ribosyltransferase), Pseudomonas aeruginosa ETA (exotoxin A), catalyses the transfer of ADP-ribose from NAD+ to its protein substrate. A series of water-soluble compounds that structurally mimic the nicotinamide moiety of NAD+ was investigated for their inhibition of the catalytic domain of ETA. The importance of an amide locked into a hetero-ring structure and a core hetero-ring system that is planar was a trend evident by the IC50 values. Also, the weaker inhibitors have core ring structures that are less planar and thus more flexible. One of the most potent inhibito

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Edmonds, C., G. E. Griffin, and A. P. Johnstone. "Demonstration and partial characterization of ADP-ribosylation in Pseudomonas maltophilia." Biochemical Journal 261, no. 1 (1989): 113–18. http://dx.doi.org/10.1042/bj2610113.

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ADP-ribosylation of proteins occurs in many eukaryotes, and it is also the mechanism of action of a growing number of important bacterial toxins. To date, however, there is only one well-characterized ADP-ribosylation system where the ADP-ribosyltransferase and the substrate protein are both bacterial in origin, namely within the nitrogen-fixing bacterium Rhodospirillum rubrum. The present paper demonstrates the endogenous ADP-ribosylation of two proteins of Mr 32,000 and 20,000 within Pseudomonas maltophilia, a Gram-negative aerobe. The proteins have been partially purified: two apparently se

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Qi, Hongyun, Brendan D. Price, and Tovah A. Day. "Multiple Roles for Mono- and Poly(ADP-Ribose) in Regulating Stress Responses." Trends in Genetics 35, no. 2 (2019): 159–72. http://dx.doi.org/10.1016/j.tig.2018.12.002.

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Zapata-Pérez, Rubén, Fernando Gil-Ortiz, Ana Belén Martínez-Moñino, Antonio Ginés García-Saura, Jordi Juanhuix, and Álvaro Sánchez-Ferrer. "Structural and functional analysis of Oceanobacillus iheyensis macrodomain reveals a network of waters involved in substrate binding and catalysis." Open Biology 7, no. 4 (2017): 160327. http://dx.doi.org/10.1098/rsob.160327.

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Macrodomains are ubiquitous conserved domains that bind or transform ADP-ribose (ADPr) metabolites. In humans, they are involved in transcription, X-chromosome inactivation, neurodegeneration and modulating PARP1 signalling, making them potential targets for therapeutic agents. Unfortunately, some aspects related to the substrate binding and catalysis of MacroD-like macrodomains still remain unclear, since mutation of the proposed catalytic aspartate does not completely abolish enzyme activity. Here, we present a functional and structural characterization of a macrodomain from the extremely ha

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Piron, K. J., and K. K. McMahon. "Localization and partial characterization of ADP-ribosylation products in hearts from adult and neonatal rats." Biochemical Journal 270, no. 3 (1990): 591–97. http://dx.doi.org/10.1042/bj2700591.

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The subcellular distributions of endogenous ADP-ribosylation products in hearts from 1-day-old neonatal and adult rats were investigated. In adult rat heart a 52 kDa mono-ADP-ribosylation product was identified in the plasma membrane fraction. In contrast, in neonatal rat heart a 130 kDa poly-ADP-ribosylation product was present in the nuclear fraction. The monomeric and polymeric nature of the two ADP-ribosylation products was determined by their sensitivity to thymidine and by analysis of their snake venom phosphodiesterase products. NADP+ enhanced both the mono- and polymeric reactions. The

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GRAHNERT, Andreas, Maik FRIEDRICH, Martin PFISTER, Friedrich HAAG, Friedrich KOCH-NOLTE, and Sunna HAUSCHILDT. "Mono-ADP-ribosyltransferases in human monocytes: regulation by lipopolysaccharide." Biochemical Journal 362, no. 3 (2002): 717–23. http://dx.doi.org/10.1042/bj3620717.

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ADP-ribosyltransferase activity was shown to be present on the surface of human monocytes. Incubating the cells in the presence of BSA leads to an increase in enzyme activity. The acceptor amino acid mainly responsible for the ADP-ribose bond was identified as a cysteine residue. An increase in ADP-ribosyltransferase activity was observed when cells were treated for 16h with bacterial lipopolysaccharide (LPS). Possible candidates for catalysing the reaction are mono-ADP-ribosyltransferases (ARTs). When measuring expression of the mRNA of ART1, 3, 4 and 5, only ART3 mRNA was detected in unstimu

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Crawford, Kerryanne, Peter L. Oliver, Thomas Agnew, Benjamin H. M. Hunn, and Ivan Ahel. "Behavioural Characterisation of Macrod1 and Macrod2 Knockout Mice." Cells 10, no. 2 (2021): 368. http://dx.doi.org/10.3390/cells10020368.

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Adenosine diphosphate ribosylation (ADP-ribosylation; ADPr), the addition of ADP-ribose moieties onto proteins and nucleic acids, is a highly conserved modification involved in a wide range of cellular functions, from viral defence, DNA damage response (DDR), metabolism, carcinogenesis and neurobiology. Here we study MACROD1 and MACROD2 (mono-ADP-ribosylhydrolases 1 and 2), two of the least well-understood ADPr-mono-hydrolases. MACROD1 has been reported to be largely localized to the mitochondria, while the MACROD2 genomic locus has been associated with various neurological conditions such as

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Kamata, Teddy, Chun-Song Yang, and Bryce M. Paschal. "PARP7 mono-ADP-ribosylates the agonist conformation of the androgen receptor in the nucleus." Biochemical Journal 478, no. 15 (2021): 2999–3014. http://dx.doi.org/10.1042/bcj20210378.

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We recently described a signal transduction pathway that contributes to androgen receptor (AR) regulation based on site-specific ADP-ribosylation by PARP7, a mono-ADP-ribosyltransferase implicated in several human cancers. ADP-ribosylated AR is recognized by PARP9/DTX3L, a heterodimeric complex that contains an ADP-ribose reader (PARP9) and a ubiquitin E3 ligase (DTX3L). Here, we have characterized the cellular and biochemical requirements for AR ADP-ribosylation by PARP7. We found that the reaction requires nuclear localization of PARP7 and an agonist-induced conformation of AR. PARP7 contain

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Vatta, Maritza, Bronwyn Lyons, Kayla A. Heney, Taylor Lidster, and A. Rod Merrill. "Mapping the DNA-Binding Motif of Scabin Toxin, a Guanine Modifying Enzyme from Streptomyces scabies." Toxins 13, no. 1 (2021): 55. http://dx.doi.org/10.3390/toxins13010055.

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Scabin is a mono-ADP-ribosyltransferase toxin/enzyme and possible virulence factor produced by the agriculture pathogen, Streptomyces scabies. Recently, molecular dynamic approaches and MD simulations revealed its interaction with both NAD+ and DNA substrates. An Essential Dynamics Analysis identified a crab-claw-like mechanism, including coupled changes in the exposed motifs, and the Rβ1-RLa-NLc-STTβ2-WPN-WARTT-(QxE)ARTT sequence motif was proposed as a catalytic signature of the Pierisin family of DNA-acting toxins. A new fluorescence assay was devised to measure the kinetics for both RNA an

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Okazaki, IJ, HJ Kim, NG McElvaney, E. Lesma, and J. Moss. "Molecular characterization of a glycosylphosphatidylinositol-linked ADP- ribosyltransferase from lymphocytes." Blood 88, no. 3 (1996): 915–21. http://dx.doi.org/10.1182/blood.v88.3.915.915.

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Abstract Mono ADP-ribosyltransferases catalyze the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD) to proteins. It was reported by Wang et al (J Immunol 153:4048, 1994) that incubation of mouse cytotoxic T lymphocytes (CTL) with NAD resulted in the ADP- ribosylation of membrane proteins and inhibition of cell proliferation and cytotoxicity. Treatment of CTL with phosphatidylinositol-specific phospholipase C (PI-PLC) before incubation with NAD prevented the inhibitory effects of NAD on the cells, consistent with the removal of a glycosylphosphatidylinositol (GPI)-an

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Okazaki, IJ, HJ Kim, NG McElvaney, E. Lesma, and J. Moss. "Molecular characterization of a glycosylphosphatidylinositol-linked ADP- ribosyltransferase from lymphocytes." Blood 88, no. 3 (1996): 915–21. http://dx.doi.org/10.1182/blood.v88.3.915.bloodjournal883915.

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Mono ADP-ribosyltransferases catalyze the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD) to proteins. It was reported by Wang et al (J Immunol 153:4048, 1994) that incubation of mouse cytotoxic T lymphocytes (CTL) with NAD resulted in the ADP- ribosylation of membrane proteins and inhibition of cell proliferation and cytotoxicity. Treatment of CTL with phosphatidylinositol-specific phospholipase C (PI-PLC) before incubation with NAD prevented the inhibitory effects of NAD on the cells, consistent with the removal of a glycosylphosphatidylinositol (GPI)-anchored AD

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Munnur, Deeksha, Edward Bartlett, Petra Mikolčević, et al. "Reversible ADP-ribosylation of RNA." Nucleic Acids Research 47, no. 11 (2019): 5658–69. http://dx.doi.org/10.1093/nar/gkz305.

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Abstract ADP-ribosylation is a reversible chemical modification catalysed by ADP-ribosyltransferases such as PARPs that utilize nicotinamide adenine dinucleotide (NAD+) as a cofactor to transfer monomer or polymers of ADP-ribose nucleotide onto macromolecular targets such as proteins and DNA. ADP-ribosylation plays an important role in several biological processes such as DNA repair, transcription, chromatin remodelling, host-virus interactions, cellular stress response and many more. Using biochemical methods we identify RNA as a novel target of reversible mono-ADP-ribosylation. We demonstrat

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Moss, J., M. K. Jacobson, and S. J. Stanley. "Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme." Proceedings of the National Academy of Sciences 82, no. 17 (1985): 5603–7. http://dx.doi.org/10.1073/pnas.82.17.5603.

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Stabb, Eric V., Karl A. Reich, and Edward G. Ruby. "Vibrio fischeri Genes hvnA andhvnB Encode Secreted NAD+-Glycohydrolases." Journal of Bacteriology 183, no. 1 (2001): 309–17. http://dx.doi.org/10.1128/jb.183.1.309-317.2001.

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ABSTRACT HvnA and HvnB are proteins secreted by Vibrio fischeriES114, an extracellular light organ symbiont of the squidEuprymna scolopes, that catalyze the transfer of ADP-ribose from NAD+ to polyarginine. Based on this activity, HvnA and HvnB were presumptively designated mono-ADP-ribosyltransferases (ARTases), and it was hypothesized that they mediate bacterium-host signaling. We have clonedhvnA and hvnB from strain ES114.hvnA appears to be expressed as part of a four-gene operon, whereas hvnB is monocistronic. The predicted HvnA and HvnB amino acid sequences are 46% identical to one anothe

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Saxty, B. A., and S. van Heyningen. "The purification of a cysteine-dependent NAD+ glycohydrolase activity from bovine erythrocytes and evidence that it exhibits a novel ADP-ribosyltransferase activity." Biochemical Journal 310, no. 3 (1995): 931–37. http://dx.doi.org/10.1042/bj3100931.

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An NAD+:cysteine ADP-ribosyltransferase activity was purified from bovine erythrocytes on the assumption that, like pertussis toxin, the enzyme would exhibit a cysteine-dependent NAD+ glycohydrolase activity. A three-step purification procedure was developed involving (1) precipitation with 40% (NH4)2SO4, (2) binding to a cysteine-Sepharose affinity column, and (3) binding to an NAD+ affinity column. PAGE showed a single band of M(r) 45,000. The enzyme had been purified 47,000-fold and had a specific activity of 1900 nmol nicotinamide released/min per mg. A study of the kinetic properties of t

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Aboul-Ela, Nasreen, Elaine L. Jacobson, and Myron K. Jacobson. "Labeling methods for the study of poly- and mono(ADP-ribose) metabolism in cultured cells." Analytical Biochemistry 174, no. 1 (1988): 239–50. http://dx.doi.org/10.1016/0003-2697(88)90541-6.

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Heer, Collin D., Daniel J. Sanderson, Lynden S. Voth, et al. "Coronavirus infection and PARP expression dysregulate the NAD metabolome: An actionable component of innate immunity." Journal of Biological Chemistry 295, no. 52 (2020): 17986–96. http://dx.doi.org/10.1074/jbc.ra120.015138.

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Poly(ADP-ribose) polymerase (PARP) superfamily members covalently link either a single ADP-ribose (ADPR) or a chain of ADPR units to proteins using NAD as the source of ADPR. Although the well-known poly(ADP-ribosylating) (PARylating) PARPs primarily function in the DNA damage response, many noncanonical mono(ADP-ribosylating) (MARylating) PARPs are associated with cellular antiviral responses. We recently demonstrated robust up-regulation of several PARPs following infection with murine hepatitis virus (MHV), a model coronavirus. Here we show that SARS-CoV-2 infection strikingly up-regulates

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García-Saura, Antonio Ginés, and Herwig Schüler. "PARP10 Multi-Site Auto- and Histone MARylation Visualized by Acid-Urea Gel Electrophoresis." Cells 10, no. 3 (2021): 654. http://dx.doi.org/10.3390/cells10030654.

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Poly-ADP-ribose polymerase (PARP)-family ADP-ribosyltransferases function in various signaling pathways, predominantly in the nucleus and cytosol. Although PARP inhibitors are in clinical practice for cancer therapy, the enzymatic activities of individual PARP family members are yet insufficiently understood. We studied PARP10, a mono-ADP-ribosyltransferase and potential drug target. Using acid-urea gel electrophoresis, we found that the isolated catalytic domain of PARP10 auto-ADP-ribosylates (MARylates) at eight or more acceptor residues. We isolated individual species with either singular o

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