ArticleNucleic acids research2005
A highly specific phosphatase that acts on ADP-ribose 1''-phosphate, a metabolite of tRNA splicing in Saccharomyces cerevisiae.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 57 citations in OpenAlex.
- Apprehending the NADViruses · 2022Article
- Beyond protein modification: the rise of non-canonical ADP-ribosylation.The Biochemical journal · 2022Article
- ADP-ribosylhydrolases: from DNA damage repair to COVID-19.Journal of Zhejiang University. Science. B · 2021Review
- The SARS-CoV-2 Conserved Macrodomain Is a Mono-ADP-Ribosylhydrolase.Journal of virology · 2021Article
- Jumbo Phages: A Comparative Genomic Overview of Core Functions and Adaptions for Biological Conflicts.Viruses · 2021Article
- An uncharacterized FMAG_01619 protein from Fusobacterium mortiferum ATCC 9817 demonstrates that some bacterial macrodomains can also act as poly-ADP-ribosylhydrolases.Scientific reports · 2019Article
- Viral Macrodomains: Unique Mediators of Viral Replication and Pathogenesis.Trends in microbiology · 2018Review
- ADP-ribosylation: new facets of an ancient modification.The FEBS journal · 2017Review
- RNA damage in biological conflicts and the diversity of responding RNA repair systems.Nucleic acids research · 2016Review
- Viral Macro Domains Reverse Protein ADP-Ribosylation.Journal of virology · 2016Article
- Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module: CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES.The Journal of biological chemistry · 2016Article
- Nudix hydrolases degrade protein-conjugated ADP-ribose.Scientific reports · 2015Article
- Article
- The nsp3 macrodomain promotes virulence in mice with coronavirus-induced encephalitis.Journal of virology · 2015Article
- Macrodomain-containing proteins: regulating new intracellular functions of mono(ADP-ribosyl)ation.Nature reviews. Molecular cell biology · 2013Review
- A genetic screen for high copy number suppressors of the synthetic lethality between elg1Δ and srs2Δ in yeast.G3 (Bethesda, Md.) · 2013Article
- Genomics-guided analysis of NAD recycling yields functional elucidation of COG1058 as a new family of pyrophosphatases.PloS one · 2013Article
- Molecular Insights into Poly(ADP-ribose) Recognition and Processing.Biomolecules · 2012Article
- Understanding the alphaviruses: recent research on important emerging pathogens and progress towards their control.Antiviral research · 2010Review
- Presence of a classical RRM-fold palm domain in Thg1-type 3'- 5'nucleic acid polymerases and the origin of the GGDEF and CRISPR polymerase domains.Biology direct · 2010Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
One molecule of ADP-ribose 1'',2''-cyclic phosphate (Appr>p) is formed during each of the approximately 500 000 tRNA splicing events per Saccharomyces cerevisiae generation. The metabolism of Appr>p remains poorly defined. A cyclic phosphodiesterase (Cpd1p) has been shown to convert Appr>p to ADP-ribose-1''-phosphate (Appr1p). We used a biochemical genomics approach to identify two yeast phosphatases that can convert Appr1p to ADP-ribose: the product of ORF YBR022w (now Poa1p), which is completely unrelated to other known phosphatases; and Hal2p, a known 3'-phosphatase of 5',3'-pAp. Poa1p is highly specific for Appr1p, and thus likely acts on this molecule in vivo. Poa1 has a relatively low K(M) for Appr1p (2.8 microM) and a modest kcat (1.7 min(-1)), but no detectable activity on several other substrates. Furthermore, Poa1p is strongly inhibited by ADP-ribose (K(I), 17 microM), modestly inhibited by other nucleotides containing an ADP-ribose moiety and not inhibited at all by other tested molecules. In contrast, Hal2p is much more active on pAp than on Appr1p, and several other tested molecules were Hal2p substrates or inhibitors. poa1-Delta mutants have no obvious growth defect at different temperatures in rich media, and analysis of yeast extracts suggests that approximately 90% of Appr1p processing activity originates from Poa1p.
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