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The Dichotomy of the Poly(ADP-Ribose) Polymerase-Like Thermozyme from Sulfolobus solfataricus
Full text linkThe first evidence of an ADP-ribosylating activity in Archaea was obtained in Sulfolobus solfataricus(strain MT-4) where a poly(ADP-ribose) polymerase (PARP)-like thermoprotein, defined with the acronymous PARPSso, was found. Similarly to the eukaryotic counterparts PARPSso cleaves beta-nicotinamide adenine dinucleotide to synthesize oligomers of ADP-ribose; cross-reacts with polyclonal anti-PARP-1 catalytic site antibodies; binds DNA. The main differences rely on the molecular mass (46.5 kDa) and the thermophily of PARPSso which works at 80 °C. Despite the biochemical properties that allow correlating it to PARP enzymes, the N-terminal and partial amino acid sequences available suggest that PARPSso belongs to a different group of enzymes, the DING proteins, an item discussed in detail in this review.This finding makes PARPSso the first example of a DING protein in Archaea and extends the existence of DING proteins into all the biological kingdoms. PARPSsohas a cell peripheral localization, along with the edge of the cell membrane. The ADP-ribosylation reaction is reverted by a poly(ADP-ribose) glycohydrolase-like activity, able to use the eukaryotic poly(ADP-ribose) as a substrate too. Here we overview the research of (ADP-ribosyl)ation in Sulfolobus solfataricus in the past thirty years and discuss the features of PARPSso common with the canonical poly(ADP-ribose) polymerases, and the structure fitting with that of DING proteins
Past and current Topics on ADPribosylation reactions
No full textThe milestone of Adenosine Diphosphate-ribosylation studies was the paper by Paul Mandel’s group in 1960s, first describing a “sort” of polyadenylic acid synthesized upon addition of nicotinamide mononucleotide in rat liver nuclear extracts. Nicotinic Acid or Niacin is the precursor of Nicotinamide Adenin Dinucleotide. In 1960s this compound was known mainly as coenzyme of most redox processes in metabolism. The discovery of enzymes that covalently transfer Adenosine Diphosphate-ribose moiety of Nicotinamide Adenin Dinucleotide to acceptor proteins, thereby altering their function, or are able to synthesize cyclic Adenosine Diphosphate-ribose, has given rise to the era of one of the most studied and still surprising reversible post – translational modification reactions. Over 50 years, developing the research on Adenosine Diphosphate-ribosylation has provided the basis to interconnect several processes thought to be very distant each other, opening new perspectives in their regulation and in therapeutic intervention. Here a synthesis of the history and the main and recent goals reached studying Adenosine Diphosphate-ribose in all its features are provided by a series of reviews including the most advanced research
14th world congress on advances in Oncology and 12th international symposium on molecular medicine
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The evolution of ADP-ribosylating enzymes and the wide spectrum of their biological significance - Special Issue
No full textA new facet of ADP-ribosylation reactions: SIRTs and PARPs Interplay
No full textNicotinamide Adenine Dinucleotide (NAD+) is mainly known as coenzyme of redox reactions for energy transduction and is consumed as substrate in regulatory reactions removing nicotinamide and producing ADP-ribose. Several families of ADP-ribose synthesizing enzymes use NAD+ as substrate and control processes like DNA repair, replication and transcription, chromatin structure, the activity of G-proteins and others. Since NAD+-dependent reactions involve degradation of the dinucleotide, a constant supply of the pyridinic substrate is required for its homeostasis. NAD+-dependent signaling reactions include protein deacetylation by sirtuins, intracellular calcium signaling and mono-/poly-ADP-ribosylation. In the context of all NAD+-dependent reactions leading to ADP-ribose synthesis, this review focuses mainly on both the central role played by sirtuins and poly-ADPribose polymerases as cellular NAD+ consumers and their crosstalk in signaling pathways
IN THE THERMOPHILIC ARCHAEON S.SOLFATARICUS A DNA-BINDING PROTEIN IS IN VITRO ADPRIBOSYLATED
No full textCHROMATIN ARCHITECTURE AND FUNCTIONS: THE ROLE(S) OF POLY(ADP-RIBOSE) POLYMERASE AND POLY(ADPRIBOSYL)ATION OF NUCLEAR PROTEINS.
No full textSPECIAL EPIGENETIC ISSUE
Epigenetic states that allow chromatin fidelity inheritance can be mediated by several factors. One of them, histone variants and their modifications (including acetylation, methylation, phosphorylation, poly(ADP-ribosyl)ation, and ubiquitylation) create distinct patterns of signals read by other proteins, and are strictly related to chromatin remodelling, which is necessary for the specific expression of a gene, and for DNA repair, recombination, and replication. In the framework of chromatin-controlling factors, the poly(ADP-ribosyl)ation of nuclear proteins, catalysed by poly(ADP-ribose)polymerases (PARPs), has been implicated in the regulation of both physiological and pathological events (gene expression/amplification, cellular division/differentiation, DNA replication, malignant transformation, and apoptotic cell death). The involvement of PARPs in this scenario has raised doubts about the epigenetic value of poly(ADP-ribosyl)ation, because it is generally activated after DNA damage. However, one emerging view suggests that both the product of this reaction, poly(ADP-ribose), and PARPs, particularly PARP 1, play a fundamental role in recruiting protein targets to specific sites and (or) in interacting physically with structural and regulatory factors, through highly reproducible and inheritable mechanisms, often independent of DNA breaks. The interplay of PARPs with protein factors, and the combinatorial effect of poly(ADPribosyl)ation with other post-translational modifications has shed new light on the potential and versatility of this dynamic reaction
IN THE THERMOPHILIC ARCHAEON S.SOLFATARICUS A DNA-BINDING PROTEIN IS IN VITRO ADPRIBOSYLATED
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