Selective monitoring of the protein-free ADP-ribose released by ADP-ribosylation reversal enzymes
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) a...
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| creator | Kasson, Samuel Dharmapriya, Nuwani Kim, In-Kwon |
| description | 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 NUDT5-coupled AMP-Glo (NCAG) assay to specifically monitor the protein-free ADP-ribose released by ADP-ribosylation reversal enzymes. We found that NUDT5 selectively cleaves protein-free ADP-ribose, but not protein-bound poly- and mono-ADP-ribosylations, protein-free poly(ADP-ribose) chains, or NAD.sup.+ . As a proof-of-concept, we successfully measured the kinetic parameters for the exo-glycohydrolase activity of PARG, which releases monomeric ADP-ribose, and monitored activities of site-specific mono-ADP-ribosyl-acceptor hydrolases, such as ARH3 and TARG1. This NCAG assay can be used as a general platform to study the mechanisms of diverse ADP-ribosylation reversal enzymes that release protein-free ADP-ribose as a product. Furthermore, this assay provides a useful tool to identify small-molecule probes targeting ADP-ribosylation metabolism and to quantify ADP-ribose concentrations in cells. |
| doi_str_mv | 10.1371/journal.pone.0254022 |
| format | Article |
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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 NUDT5-coupled AMP-Glo (NCAG) assay to specifically monitor the protein-free ADP-ribose released by ADP-ribosylation reversal enzymes. We found that NUDT5 selectively cleaves protein-free ADP-ribose, but not protein-bound poly- and mono-ADP-ribosylations, protein-free poly(ADP-ribose) chains, or NAD.sup.+ . As a proof-of-concept, we successfully measured the kinetic parameters for the exo-glycohydrolase activity of PARG, which releases monomeric ADP-ribose, and monitored activities of site-specific mono-ADP-ribosyl-acceptor hydrolases, such as ARH3 and TARG1. This NCAG assay can be used as a general platform to study the mechanisms of diverse ADP-ribosylation reversal enzymes that release protein-free ADP-ribose as a product. Furthermore, this assay provides a useful tool to identify small-molecule probes targeting ADP-ribosylation metabolism and to quantify ADP-ribose concentrations in cells.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0254022</identifier><identifier>PMID: 34191856</identifier><language>eng</language><publisher>San Francisco: Public Library of Science</publisher><subject>Adenosine diphosphate ; ADP-ribosylation ; AMP ; Analysis ; Apoptosis ; Assaying ; Biology and Life Sciences ; Cellular stress response ; Chemistry ; Cloning ; DNA damage ; Enzymes ; Gene expression ; Medicine and Health Sciences ; Metabolism ; NAD ; Physical sciences ; Plasmids ; Poly(ADP-ribose) ; Poly(ADP-ribose) glycohydrolase ; Poly(ADP-ribose) polymerase ; Post-translation ; Post-translational modification ; Protein binding ; Proteins ; Research and Analysis Methods ; Ribose ; Ribosylation</subject><ispartof>PloS one, 2021-06, Vol.16 (6), p.e0254022-e0254022</ispartof><rights>COPYRIGHT 2021 Public Library of Science</rights><rights>2021 Kasson et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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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 NUDT5-coupled AMP-Glo (NCAG) assay to specifically monitor the protein-free ADP-ribose released by ADP-ribosylation reversal enzymes. We found that NUDT5 selectively cleaves protein-free ADP-ribose, but not protein-bound poly- and mono-ADP-ribosylations, protein-free poly(ADP-ribose) chains, or NAD.sup.+ . As a proof-of-concept, we successfully measured the kinetic parameters for the exo-glycohydrolase activity of PARG, which releases monomeric ADP-ribose, and monitored activities of site-specific mono-ADP-ribosyl-acceptor hydrolases, such as ARH3 and TARG1. This NCAG assay can be used as a general platform to study the mechanisms of diverse ADP-ribosylation reversal enzymes that release protein-free ADP-ribose as a product. Furthermore, this assay provides a useful tool to identify small-molecule probes targeting ADP-ribosylation metabolism and to quantify ADP-ribose concentrations in cells.</description><subject>Adenosine diphosphate</subject><subject>ADP-ribosylation</subject><subject>AMP</subject><subject>Analysis</subject><subject>Apoptosis</subject><subject>Assaying</subject><subject>Biology and Life Sciences</subject><subject>Cellular stress response</subject><subject>Chemistry</subject><subject>Cloning</subject><subject>DNA damage</subject><subject>Enzymes</subject><subject>Gene expression</subject><subject>Medicine and Health Sciences</subject><subject>Metabolism</subject><subject>NAD</subject><subject>Physical sciences</subject><subject>Plasmids</subject><subject>Poly(ADP-ribose)</subject><subject>Poly(ADP-ribose) glycohydrolase</subject><subject>Poly(ADP-ribose) polymerase</subject><subject>Post-translation</subject><subject>Post-translational modification</subject><subject>Protein 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glycohydrolase</topic><topic>Poly(ADP-ribose) polymerase</topic><topic>Post-translation</topic><topic>Post-translational modification</topic><topic>Protein binding</topic><topic>Proteins</topic><topic>Research and Analysis Methods</topic><topic>Ribose</topic><topic>Ribosylation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kasson, Samuel</creatorcontrib><creatorcontrib>Dharmapriya, Nuwani</creatorcontrib><creatorcontrib>Kim, In-Kwon</creatorcontrib><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts 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Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kasson, Samuel</au><au>Dharmapriya, Nuwani</au><au>Kim, In-Kwon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Selective monitoring of the protein-free ADP-ribose released by ADP-ribosylation reversal enzymes</atitle><jtitle>PloS one</jtitle><date>2021-06-30</date><risdate>2021</risdate><volume>16</volume><issue>6</issue><spage>e0254022</spage><epage>e0254022</epage><pages>e0254022-e0254022</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>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 NUDT5-coupled AMP-Glo (NCAG) assay to specifically monitor the protein-free ADP-ribose released by ADP-ribosylation reversal enzymes. We found that NUDT5 selectively cleaves protein-free ADP-ribose, but not protein-bound poly- and mono-ADP-ribosylations, protein-free poly(ADP-ribose) chains, or NAD.sup.+ . As a proof-of-concept, we successfully measured the kinetic parameters for the exo-glycohydrolase activity of PARG, which releases monomeric ADP-ribose, and monitored activities of site-specific mono-ADP-ribosyl-acceptor hydrolases, such as ARH3 and TARG1. This NCAG assay can be used as a general platform to study the mechanisms of diverse ADP-ribosylation reversal enzymes that release protein-free ADP-ribose as a product. Furthermore, this assay provides a useful tool to identify small-molecule probes targeting ADP-ribosylation metabolism and to quantify ADP-ribose concentrations in cells.</abstract><cop>San Francisco</cop><pub>Public Library of Science</pub><pmid>34191856</pmid><doi>10.1371/journal.pone.0254022</doi><tpages>e0254022</tpages><orcidid>https://orcid.org/0000-0002-2779-9735</orcidid><orcidid>https://orcid.org/0000-0003-1190-9757</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine diphosphate ADP-ribosylation AMP Analysis Apoptosis Assaying Biology and Life Sciences Cellular stress response Chemistry Cloning DNA damage Enzymes Gene expression Medicine and Health Sciences Metabolism NAD Physical sciences Plasmids Poly(ADP-ribose) Poly(ADP-ribose) glycohydrolase Poly(ADP-ribose) polymerase Post-translation Post-translational modification Protein binding Proteins Research and Analysis Methods Ribose Ribosylation |
| title | Selective monitoring of the protein-free ADP-ribose released by ADP-ribosylation reversal enzymes |
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