Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens

Rack, J.G.M.; Morra, Rosa; Barkauskaite, Eva; Kraehenbuehl, Rolf; Ariza, Antonio; Qu, Yue; Ortmayer, Mary; Leidecker, Orsolya; Cameron, David R.; Matić, Ivan; Peleg, Anton Y.; Leys, D.; Traven, Ana; Ahel, Ivan

doi:10.1016/j.molcel.2015.06.013

Cited by 78 publications

(126 citation statements)

References 46 publications

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“…There are seven sirtuin proteins operating in human cells , their primary enzymatic activity is protein deacetylation producing O ‐acetyl‐ADP‐ribose ( O AADPr) metabolite as a by‐product of its ART reaction . Sirtuins can sometimes directly modify proteins (Fig. ).…”

Section: Adp‐ribosyltransferasesmentioning

confidence: 99%

“…). Some macrodomains have also evolved enzymatic activity and are capable of hydrolysing ADP‐ribosylation (see below) . As a consequence, macrodomain‐containing proteins are involved in a diverse set of cellular functions, such as chromatin remodelling and DNA‐damage repair, oxidative stress response, metabolic processes and pathogenic mechanisms .…”

Section: Adpr‐binding Domainsmentioning

confidence: 99%

“…Studies looking either at the genomic context of ADP‐ribosylating systems or their evolution in bacteria suggest that ADP‐ribosylation might be involved in the regulation of many crucial cellular processes including bacterial persistence, oxidative stress response and adaptation to the host environment in general .…”

Section: Other Notable Adp‐ribosylation Systems In Bacteriamentioning

confidence: 99%

“…SirTM is encoded within an operon containing a modification carrier protein (GcvH‐L). GcvH‐L becomes doubly modified by two different PTMs through the actions of SirTM (ADP‐ribosylation) and another component of the operon that acts as a lipoate ligase (synthesising the protein lipoylation) . Yet another protein product of the same operon is a macrodomain protein (belonging to the MacroD‐type class), which specifically reverses the ADP‐ribosylation of GcvH‐L .…”

Section: Other Notable Adp‐ribosylation Systems In Bacteriamentioning

confidence: 99%

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ADP‐ribosylation: new facets of an ancient modification

2017

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Rapid response to environmental changes is achieved by uni‐ and multicellular organisms through a series of molecular events, often involving modification of macromolecules, including proteins, nucleic acids and lipids. Amongst these, ADP‐ribosylation is of emerging interest because of its ability to modify different macromolecules in the cells, and its association with many key biological processes, such as DNA‐damage repair, DNA replication, transcription, cell division, signal transduction, stress and infection responses, microbial pathogenicity and aging. In this review, we provide an update on novel pathways and mechanisms regulated by ADP‐ribosylation in organisms coming from all kingdoms of life.

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Section: Adp‐ribosyltransferasesmentioning

confidence: 99%

Section: Adpr‐binding Domainsmentioning

confidence: 99%

Section: Other Notable Adp‐ribosylation Systems In Bacteriamentioning

confidence: 99%

Section: Other Notable Adp‐ribosylation Systems In Bacteriamentioning

confidence: 99%

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ADP‐ribosylation: new facets of an ancient modification

2017

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“…The modification is catalyzed by a diverse family of ADP-ribosyltransferase (ART) enzymes, including (1) bacterial toxins (e.g., Cholera and Diphtheria toxins) [6, 28], (2) ecto-ADP-ribosyltransferases (ectoARTs) [10], (3) members of the sirtuin family [13, 25, 31], and (4) members of the poly(ADP-ribose) polymerase (PARP) family [2, 8]. ARTs generally catalyze mono(ADP-ribosyl)ation (MARylation) of their substrate proteins, although some PARPs, such as PARP-1, catalyze oligo- and poly(ADP-ribosyl)ation (OARylation and PARylation, respectively) [6, 8, 10, 14, 32] (Figure 1).…”

Section: Introductionmentioning

confidence: 99%

Generating Protein-Linked and Protein-Free Mono-, Oligo-, and Poly(ADP-Ribose) In Vitro

Lin

Huang

Kraus

2018

Methods in Molecular Biology

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ADP-ribosylation is a covalent posttranslational modification of proteins that is catalyzed by various types of ADP-ribosyltransferase (ART) enzymes, including members of the poly(ADP-ribose) polymerase (PARP) family. ADP-ribose (ADPR) modifications can occur as mono(ADP-ribosyl)ation, oligo(ADP-ribosyl)ation, or poly(ADP-ribosyl)ation, depending on the particular ART enzyme catalyzing the reaction, as well as the specific reaction conditions. Understanding the biology of ADP-ribosylation requires facile and robust means of generating and detecting the modification in all of its forms. Here we describe how to generate protein-linked mono(ADP-ribose), oligo(ADP-ribose), and poly(ADP-ribose) (MAR, OAR, and PAR, respectively) in vitro as an automodification of PARPs 1 or 3. First, epitope-tagged PARP-1 (a PARP polyenzyme) and PARP-3 (a PARP monoenzyme) are expressed individually in insect cells using baculovirus expression vectors, and purified using immunoaffinity chromatography. Second, the purified recombinant PARPs are incubated individually in the presence of different concentrations of NAD (as a donor of ADPR groups) and sheared DNA (to activate their catalytic activities) resulting in various forms of auto-ADP-ribosylation. Third, the products are confirmed using ADPR detection reagents that can distinguish among MAR, OAR, and PAR. Finally, if desired, the OAR and PAR can be deproteinized. The protein-linked and free MAR, OAR, and PAR generated in these reactions can be used as standards, substrates, or binding partners in a variety of ADPR-related assays.

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Molecular Tools for the Study of ADP‐Ribosylation: A Unified and Versatile Method to Synthesise Native Mono‐ADP‐Ribosylated Peptides

Voorneveld

Rack

Gijlswijk

et al. 2021

Chemistry A European J

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ADP-ribosylation (ADPr), as a post-translational modification, plays a crucial role in DNA-repair, immunity and many other cellular and physiological processes. Serine is the main acceptor for ADPr in DNA damage response, whereas the physiological impact of less common ADPr-modifications of cysteine and threonine side chains is less clear. Generally, gaining molecular insights into ADPr recognition and turnover is hampered by the availability of homogeneous, ADPribosylated material, such as mono-ADP-ribosylated (MARy-lated) peptides. Here, a new and efficient solid-phase strategy for the synthesis of Ser-, Thr-and Cys-MARylated peptides is described. ADP-ribosylated cysteine, apart from being a native post-translational modification in its own right, proved to be suitable as a stabile bioisostere for ADP-ribosylated serine making it a useful tool to further biochemical research on serine ADP-ribosylation. In addition, it was discovered that the Streptococcus pyogenes encoded protein, SpyMacroD, acts as a Cys-(ADP-ribosyl) hydrolase.

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Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens

Cited by 78 publications

References 46 publications

ADP‐ribosylation: new facets of an ancient modification

ADP‐ribosylation: new facets of an ancient modification

Generating Protein-Linked and Protein-Free Mono-, Oligo-, and Poly(ADP-Ribose) In Vitro

Molecular Tools for the Study of ADP‐Ribosylation: A Unified and Versatile Method to Synthesise Native Mono‐ADP‐Ribosylated Peptides

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