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Dive into the research topics where Maria Rosaria Faraone-Mennella is active.

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Featured researches published by Maria Rosaria Faraone-Mennella.


Molecular and Cellular Biochemistry | 2009

Poly(ADP-ribosyl)ation of proteins and germ cell development in hyperthyroid rat testes

Maria Rosaria Faraone-Mennella; Angela Ferone; Lucia Marino; Anna Cardone; Raffaella Comitato; P. Venditti; Sergio Di Meo; Benedetta Farina

The effect of increased serum levels of thyroid hormone (triiodothyronine, T3) on young rat testis spermatogenesis was studied by analysing molecular and morphological parameters. Hyperthyroidism was induced by either T3-treatment or 2- and 10-day cold exposure. The poly(ADP-ribosyl)ation of proteins catalysed by poly(ADP-ribose) polymerase, which is particularly active at specific stages of rat spermatogenesis, was analysed as molecular index of DNA damage and cell stress. Poly(ADP-ribose) polymerase activity rose after both T3-treatment and 2- and 10-day cold exposure, with a trend of 10-day cold-exposed rats towards control values. In all hyperthyroid rats poly(ADP-ribose) turnover, as a contribution of both poly(ADP-ribose) polymerase and poly(ADP-ribose) glycohydrolase), was enhanced with respect to euthyroid animals. Poly(ADP-ribosyl)ation of proteins occurred with long and branched polymers suggesting an increased involvement of the modification system in DNA repair. Morphological changes of germ tissue were observed in hyperthyroid rats, mainly a high reduction of mature cells in the seminiferous tubule, and evidence of germ cell apoptosis was obtained by TUNEL method. In control animals germ cell apoptosis was within physiological levels. Conversely, in hyperthyroid rats a dramatic increase in the number of TUNEL-positive cells (some spermatogonia and numerous primary spermatocytes) was found, even though the increase was lower in 10-day than in 2-day cold-exposed animals.


Biological Chemistry | 2009

The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein

Antimo Di Maro; Anna De Maio; Sabrina Castellano; Augusto Parente; Benedetta Farina; Maria Rosaria Faraone-Mennella

Abstract The partial amino acid sequence of the sulfolobal thermoprotein biochemically characterized as poly(ADP-ribose)polymerase-like enzyme overlaps those of DING proteins. This group of proteins, widely occurring in animals, plants and eubacteria, shows a characteristic and highly conserved N-terminus, DINGGGATL. The sequence of the N-terminal region and of the analyzed tryptic peptides of the sulfolobal thermozyme shows a high similarity with most of the DING proteins from databases. This is the first example of a DING protein from a sulfolobal source.


FEBS Letters | 2009

The ADP‐ribosylation of Sulfolobus solfataricus Sso7 modulates protein/DNA interactions in vitro

Sabrina Castellano; Benedetta Farina; Maria Rosaria Faraone-Mennella

The 7 kDa Sso7 is a basic protein particularly abundant in Sulfolobus solfataricus and is involved in DNA assembly. This protein undergoes in vitro ADP‐ribosylation by an endogenous poly(ADP‐ribose) polymerase‐like enzyme. The circular dichroism spectrum of purified ADP‐ribosylated Sso7 shows that this modification stabilizes the prevalent protein β‐conformation, as suggested by shifting of negative ellipticity minimum to 220 nm. Moreover, a short ADP‐ribose chain (up to 6‐mers) bound to Sso7 is able to reduce drastically the thermoprotective and DNA condensing ability of the protein, suggesting a possible regulatory role of ADP‐ribosylation in sulfolobal DNA organization.


Journal of Cellular Biochemistry | 2002

High stability binding of poly(ADPribose) polymerase‐like thermozyme from S. solfataricus with circular DNA

Maria Rosaria Faraone-Mennella; Paola De Luca; Anna Giordano; Agata Gambacorta; Barbara Nicolaus; Benedetta Farina

The poly(ADPribose) polymerase‐like thermozyme from the hyperthermophilic archaeon S. solfataricus was found to bind DNA with high affinity and non‐specifically. Binding was independent of base composition and length of the nucleic acid, and the protein showed a slight preference for the circular structure. By using pCMV‐Neo‐Bam plasmid as experimental model, the behaviour of the thermozyme upon binding with either circular or linear plasmid was analyzed. pCMV‐Neo‐Bam has a single HindIII site that allows to obtain the linear structure after digestion with the restriction enzyme. Intrinsic tryptophan‐dependent fluorescence of poly(ADPribose) polymerase‐like thermozyme noticeably changed upon addition of either circular or linear plasmid, showing the same binding affinity (K = 2 × 109 M−1). However, experiments of protection against temperature and DNase I gave evidence that the thermozyme formed more stable complexes with the circular structure than with the linear pCMV‐Neo‐Bam. Increasing temperature at various DNA/protein ratios had a double effect to reduce the amount of circular DNA undergoing denaturation and to split the melting point towards higher temperatures. Nil or irrelevant effect was observed with the linear form. Similarly, DNase acted preferentially on the linear plasmid/protein complexes, producing an extensive digestion even at high protein/DNA ratios, whereas the circular plasmid was protected by the thermozyme in a dose‐dependent manner. The complexes formed by archaeal poly(ADPribose) polymerase (PARPss) with the circular plasmid were visualized by bandshift experiments both with ethidium bromide staining and by labelling the circular plasmid with 32P. The stability of complexes was tested as a function of enzyme concentration and in the presence of a cold competitor and of 0.1% SDS. From the performed experiments, a number of 3–10 base pairs bound per molecule of enzyme was calculated, indicating a high frequency of binding. The presence of circular DNA was also able to increase by 80% the poly(ADPribose)polymerase‐like activity, as compared to 25% activation induced by the linear pCMV‐Neo‐Bam. J. Cell. Biochem. 85: 158–166, 2002.


Comparative Biochemistry and Physiology B | 2013

Vault-poly-ADP-ribose polymerase in the Octopus vulgaris brain: a regulatory factor of actin polymerization dynamic.

Anna De Maio; Emiliana Natale; Sergio Rotondo; Anna Di Cosmo; Maria Rosaria Faraone-Mennella

Our previous behavioural, biochemical and immunohistochemical analyses conducted in selected regions (supra/sub oesophageal masses) of the Octopus vulgaris brain detected a cytoplasmic poly-ADP-ribose polymerase (more than 90% of total enzyme activity). The protein was identified as the vault-free form of vault-poly-ADP-ribose polymerase. The present research extends and integrates the biochemical characterization of poly-ADP-ribosylation system, namely, reaction product, i.e., poly-ADP-ribose, and acceptor proteins, in the O. vulgaris brain. Immunochemical analyses evidenced that the sole poly-ADP-ribose acceptor was the octopus cytoskeleton 50-kDa actin. It was present in both free, endogenously poly-ADP-ribosylated form (70kDa) and in complex with V-poly-ADP-ribose polymerase and poly-ADP-ribose (260kDa). The components of this complex, alkali and high salt sensitive, were purified and characterized. The kind and the length of poly-ADP-ribose corresponded to linear chains of 30-35 ADP-ribose units, in accordance with the features of the polymer synthesized by the known vault-poly-ADP-ribose polymerase. In vitro experiments showed that V-poly-ADP-ribose polymerase activity of brain cytoplasmic fraction containing endogenous actin increased upon the addition of commercial actin and was highly reduced by ATP. Anti-actin immunoblot of the mixture in the presence and absence of ATP showed that the poly-ADP-ribosylation of octopus actin is a dynamic process balanced by the ATP-dependent polymerization of the cytoskeleton protein, a fundamental mechanism for synaptic plasticity.


Journal of Cellular Biochemistry | 2002

Interaction of the ADP-ribosylating enzyme from the hyperthermophilic archaeon S. solfataricus with DNA and ss-oligo deoxy ribonucleotides.

Maria Rosaria Faraone-Mennella; Gennaro Piccialli; Paola De Luca; Sabrina Castellano; Anna Giordano; Daniela Rigano; Lorenzo De Napoli; Benedetta Farina

The DNA‐binding ability of the poly‐ADPribose polymerase‐like enzyme from the extremely thermophilic archaeon Sulfolobus solfataricus was determined in the presence of genomic DNA or single stranded oligodeoxyribonucleotides. The thermozyme protected homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induced structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA. However, enzyme activity was slightly increased by DNA. Competition assays demonstrated that the protein interacted also with heterologous DNA. In order to characterize further the DNA binding properties of the archaeal enzyme, various ss‐oligodeoxyribonucleotides of different base composition, lengths (12‐mer to 24‐mer) and structure (linear and circular) were used for fluorescence titration measurements. Intrinsic fluorescence of the archaeal protein due to tryptophan (excitation at 295 nm) was measured in the presence of each oligomer at 60°C. Changes of tryptophan fluorescence were induced by all compounds in the same range of base number per enzyme molecule, but independently from the structural features of oligonucleotides, although the protein exhibited a slight preference for those adenine‐rich and circular. The binding affinities were comparable for all oligomers, with intrinsic association constants of the same order of magnitude (K = 106 M−1) in 0.01 M Na‐phosphate buffer, pH 8.0, and accounted for a “non‐specific” binding protein. Circular dichroism analysis showed that at 60°C the native protein was better organized in a secondary structure than at 20°C. Upon addition of oligonucleotides, enzyme structure was further stabilized and changed towards a β‐conformation. This effect was more marked with the circular oligomer. The analysed oligodeoxyribonucleotides slightly enhanced enzyme activity with the maximal increase of 50% as compared to the control. No activation was observed with the circular oligomer. J. Cell. Biochem. 85: 146–157, 2002.


Frontiers in Bioscience | 2015

A new facet of ADP-ribosylation reactions: SIRTs and PARPs interplay.

Maria Rosaria Faraone-Mennella

Nicotinamide Adenine Dinucleotide (NAD⁺) is known mainly 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.


Journal of Cellular Biochemistry | 2005

Yeast (ADPribosyl)ation: Revisiting a controversial question

Maria Rosaria Faraone-Mennella; Anna De Maio; Anna Petrella; Evangelia Syntichaki; Albina M. Kerbalaeva; S.M. Nasmetova; Toshkon G. Goulyamova; Benedetta Farina

The controversy about the occurrence of an (ADPribosyl)ating activity in yeast is still standing up. Here we discuss this topic on the basis of results obtained with classic experiments proposed over years as basis to characterize an (ADPribosyl)ation system in any organism. Independent results obtained in two different laboratories were in line with each other and went towards the occurrence of an active (ADPribosyl)ating system in Saccharomyces cerevisiae. In fact data collected from nuclear preparations of cultured cells matched those from bakers yeast and lyophilized yeast cells. Yeast (ADPribosyl)ating enzyme is a protein of 80–90 kDa, as determined by electrophoresis on polyacrylamide gel in sodium dodecyl sulphate, followed by immunoblotting with antibodies against anti‐poly(ADPribose) polymerase catalytic site. It synthesizes products, that, after digestion with phosphodiesterase, co‐migrates mainly with phosphoribosyl adenosine monophosphate after thin layer chromatography on silica gel plate.


Preparative Biochemistry & Biotechnology | 2000

Purification of the ADP-ribosylating enzyme from S. solfataricus by SDS-polyacrylamide gel electrophoresis and electroelution.

Maria Rosaria Faraone-Mennella; A. Discenza; Agata Gambacorta; Barbara Nicolaus; Benedetta Farina

ABSTRACT The ADPribosylating enzyme from the thermophilic archaeon S. solfataricus was purified by a simple procedure which included preparative electrophoresis on a 0.1% SDS- polyacrylamide gel. The gel slice containing the enzymatic protein was cut out and the enzyme was solubilized by electroelution. The pure enzyme was obtained by chromatography of the electroeluted sample on a DNA-Sepharose column. The purified enzyme retained both its full activity and the structuring ability as a function of temperature increase.


Journal of Cellular Biochemistry | 1997

ADPribosylation reaction by free ADPribose in Sulfolobus solfataricus, a thermophilic archaeon

Maria Rosaria Faraone-Mennella; F. De Lucia; A. De Maio; Agata Gambacorta; Barbara Nicolaus; Benedetta Farina

In the archaeon Sulfolobus solfataricus, protein ADPribosylation by free ADPribose was demonstrated by testing both [adenine‐14C(U)]ADPR and [adenine‐ 14C(U)]NAD as substrates. The occurrence of this process was shown by using specific experimental conditions. Increasing the incubation time and lowering the pH of the reaction mixture enhanced the protein glycation by free ADPribose. At pH 7.5 and 10 min incubation, the incorporation of free ADPribose into proteins was highly reduced. Under these conditions, the autoradiographic pattern showed that, among the targets of ADPribose electrophoresed after incubation with 32P‐NAD, the proteins modified by free 32P‐ADPribose mostly corresponded to high molecular mass components. Among the compounds known to inhibit the eukaryotic poly‐ADPribose polymerase, only ZnCl2 highly reduced the ADPribose incorporation from NAD into the ammonium sulphate precipitate. A 20% inhibition was measured in the presence of nicotinamide or 3‐aminobenzamide. No inhibition was observed replacing NAD with ADPR as substrate. J. Cell. Biochem. 66: 37–42, 1997.

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Dive into the Maria Rosaria Faraone-Mennella's collaboration.

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Benedetta Farina

University of Naples Federico II

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Anna De Maio

University of Naples Federico II

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Piera Quesada

University of Naples Federico II

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Carla Ferreri

National Research Council

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Maria D'Erme

Sapienza University of Rome

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Paola Caiafa

Sapienza University of Rome

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Sabrina Castellano

University of Naples Federico II

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Elena Porzio

National Research Council

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Maurizio Tamba

National Research Council

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