ArticleScientific reports2016
Proximal ADP-ribose Hydrolysis in Trypanosomatids is Catalyzed by a Macrodomain.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Roles of ADP-Ribosylation during Infection Establishment byPathogens (Basel, Switzerland) · 2023Review
- A molecular toolbox for ADP-ribosyl binding proteins.Cell reports methods · 2021Article
- Elucidating the tunability of binding behavior for the MERS-CoV macro domain with NAD metabolites.Communications biology · 2021Article
- Article
- (ADP-ribosyl)hydrolases: structure, function, and biology.Genes & development · 2020Review
- Deciphering the Nucleotide and RNA Binding Selectivity of the Mayaro Virus Macro Domain.Journal of molecular biology · 2019Article
- Macrodomain ADP-ribosylhydrolase and the pathogenesis of infectious diseases.PLoS pathogens · 2018Article
- Quantitative Determination of MAR Hydrolase Residue Specificity In Vitro by Tandem Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Structural and functional analysis ofOpen biology · 2017Article
- The macro domain as fusion tag for carrier-driven crystallization.Protein science : a publication of the Protein Society · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ADP-ribosylation is a ubiquitous protein modification utilized by both prokaryotes and eukaryotes for several cellular functions, such as DNA repair, proliferation, and cell signaling. Higher eukaryotes, such as humans, utilize various enzymes to reverse the modification and to regulate ADP-ribose dependent signaling. In contrast, some lower eukaryotes, including trypanosomatids, lack many of these enzymes and therefore have a much more simplified ADP-ribose metabolism. Here we identified and characterized ADP-ribose hydrolases from Trypanosoma brucei and Trypanosoma cruzi, which are homologous to human O-acetyl-ADP-ribose deacetylases MacroD1 and MacroD2. The enzymes are capable for hydrolysis of protein linked ADP-ribose and a product of sirtuin-mediated lysine deacetylation, O-acetyl-ADP-ribose. Crystal structures of the trypanosomatid macrodomains revealed a conserved catalytic site with distinct differences to human MacroD1 and MacroD2.
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