ArticleThe Biochemical journal1998
Purification and biochemical characterization of a poly(ADP-ribose) polymerase-like enzyme from the thermophilic archaeon Sulfolobus solfataricus.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 46 citations in OpenAlex.
- Shell Matrix Protein N38 of Pinctada fucata, Inducing Vaterite Formation, Extends the DING Protein to the Mollusca World.Marine biotechnology (New York, N.Y.) · 2022Article
- ADP-Ribosylation Post-Translational Modification: An Overview with a Focus on RNA Biology and New Pharmacological Perspectives.Biomolecules · 2022Review
- DING Proteins Extend to the Extremophilic World.International journal of molecular sciences · 2021Review
- InMicroorganisms · 2020Article
- Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins.Nucleic acids research · 2019Review
- ADP-ribosylation: new facets of an ancient modification.The FEBS journal · 2017Review
- The PARP family: insights into functional aspects of poly (ADP-ribose) polymerase-1 in cell growth and survival.Cell proliferation · 2016Review
- Post-translational environmental switch of RadA activity by extein-intein interactions in protein splicing.Nucleic acids research · 2015Article
- Article
- Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?Microbiology and molecular biology reviews : MMBR · 2006Review
- Purification and characterization of 5'-methylthioadenosine phosphorylase from the hyperthermophilic archaeon Pyrococcus furiosus: substrate specificity and primary structure analysis.Extremophiles : life under extreme conditions · 2003Article
- Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.Microbiology and molecular biology reviews : MMBR · 2001Review
- Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions.The Biochemical journal · 1999Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A poly(ADP-ribose) polymerase-like enzyme, detected in a crude homogenate from Sulfolobus solfataricus by means of activity and immunoblot analyses, was purified to electrophoretic homogeneity by a rapid procedure including two sequential affinity chromatographies, on NAD+-agarose and DNA-Sepharose. The latter column selected specifically the poly(ADP-ribosyl)ating enzyme with a 17% recovery of enzymic activity and a purification of more than 15000-fold. The molecular mass (54-55 kDa) assessed by SDS/PAGE and immunoblot was definitely lower than that determined for the corresponding eukaryotic protein. The enzyme was proved to be thermophilic, with a temperature optimum of approx. 80 degreesC, and thermostable, with a half-life of 204 min at 80 degreesC, in good agreement with the requirements of a thermozyme. It displayed a Km towards NAD+ of 154+/-50 microM; in the pH range 6.5-10.0 the activity values were similar, not showing a real optimum pH. The enzyme was able to bind homologous DNA, as evidenced by the ethidium bromide displacement assay. The product of the ADP-ribosylating reaction co-migrated with the short oligomers of ADP-ribose (less than 6 residues) from a eukaryotic source. Reverse-phase HPLC analysis of the products, after digestion with phosphodiesterase I, gave an elution profile reproducing that obtained by the enzymic digestion of the rat testis poly(ADP-ribose). These results strongly suggest that the activities of the purified enzyme include the elongation step.
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