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Your search keyword '"M. Rosaria Faraone-Mennella"' showing total 3 results
Start Over Author "M. Rosaria Faraone-Mennella" Topic adp-ribosylation
3 results on '"M. Rosaria Faraone-Mennella"'

1. ADP-ribosylation reactions in Sulfolobus solfataricus, a thermoacidophilic archaeon

Author

Anna De Maio, Piera Quesada, Barbara Nicolaus, Agata Gambacorta, Filomena De Lucia, Mario De Rosa, M. Rosaria Faraone-Mennella, Benedetta Farina, Faraone Mennella, Mr, De Lucia, F, De Maio, A, Gambacorta, A, Quesada, P, DE ROSA, Mario, Nicolaus, B, Farina, B., M., Rosaria Faraone Mennella, Filomena De, Lucia, DE MAIO, Anna, Agata, Gambacorta, Piera, Quesada, Mario De, Rosa, Barbara, Nicolau, and Benedetta, Farina

Subjects
sulfolobus solfataricu, Time Factors, Ribose, ved/biology.organism_classification_rank.species, Biophysics, Biology, Biochemistry, Sulfolobus, NAD+ Nucleosidase, Structural Biology, Molecular Biology, Polyacrylamide gel electrophoresis, Thermostability, chemistry.chemical_classification, ved/biology, Thermophile, Sulfolobus solfataricus, Temperature, NAD, Adenosine Diphosphate, Enzyme, chemistry, ADP-ribosylation, NAD+ kinase, NAD glycohydrolase activity
Abstract

An ADP-ribosylating system was detected in a crude homogenate from Sulfolobus solfataricus, a thermophilic archaeon, optimally growing at 87 degrees C. The archaeal ADP-ribosylation reaction was time-, temperature- and NAD-dependent. It proved to be highly thermostable, with about 30% decrease of 14C incorporation from [14C]NAD on incubation at 80 degrees C for up to 24 h. The main reaction product was found to be mono-ADP-ribose. Testing both [adenine-14C(U)]NAD and [adenine-14C(U)]ADPR as substrates, it was found that acceptor proteins were modified by ADP-ribose both enzymatically, via ADP-ribosylating enzymes, and via chemical attachment of free ADP-ribose, likely produced by NAD glycohydrolase activity. The synthesis of ADP-ribose-protein complexes was shown to involve mainly acceptors with molecular masses in the 40-100 kDa range, as determined by electrophoresis on polyacrylamide gel in the presence of sodium dodecyl sulphate.

Published
1995

2. In vitro poly(ADPribosylation) of estrogen-induced proteins from the oviduct of the lizard Podarcis s. sicula Raf

Author

Anna Cardone, Piera Quesada, Benedetta Farina, Maria Malanga, Gaetano Ciarcia, M. Rosaria Faraone-Mennella, Quesada, P, Ciarcia, Gaetano, FARAONE MENNELLA, MARIA ROSARIA, Malanga, M, Cardone, A, and Farina, B.

Subjects
Electrophoresis, endocrine system, medicine.medical_specialty, Poly Adenosine Diphosphate Ribose, Biophysics, Oviducts, Biology, In Vitro Techniques, Biochemistry, Structural Biology, Internal medicine, Histone H2B, medicine, Animals, Amino Acids, Molecular Biology, Chromatography, High Pressure Liquid, Gel electrophoresis, chemistry.chemical_classification, Podarcis, Nuclear Proteins, Estrogens, Lizards, biology.organism_classification, Ribonucleoproteins, Small Nuclear, Molecular biology, In vitro, Cell nucleus, medicine.anatomical_structure, Endocrinology, Enzyme, chemistry, Ribonucleoproteins, ADP-ribosylation, Oviduct
Abstract

Poly(ADPribosylation) of nuclear proteins has been investigated in the nuclei from growing oviducts of intact and estrogen-treated spayed females of the lizard Podarcis s. sicula Raf. Isolated nuclei were incubated with [14C]NAD and nuclear proteins extracted in 0.2 M H2SO4. Labeled acid-soluble proteins were analysed by reverse-phase high-performance liquid chromatography (HPLC) and acetic acid-urea gel electrophoresis. The results reported here indicate that the ADPribosylation reaction is involved in modifying, besides histone H2b, tissue specific proteins (SNPs and LMG-O). Moreover, comparable results have been obtained from nuclei prepared from the fully active oviduct of intact animals and spayed lizards stimulated with 17β-estradiol. It is concluded that the poly-(ADPribosylation) of hormone-induced proteins might play a role in the differentiation of the lizard oviduct.

Published
1991

3. Immunochemical detection of ADP-ribosylating enzymes in the archaeon Sulfolobus solfataricus

Author

Agata Gambacorta, Barbara Nicolaus, M. Rosaria Faraone-Mennella, and Benedetta Farina

Subjects
Male, Thermophiles, Blotting, Western, ved/biology.organism_classification_rank.species, Immunoblotting, Biophysics, Enzyme-Linked Immunosorbent Assay, Biochemistry, Sulfolobus, Western blot, Structural Biology, Testis, Escherichia coli, Genetics, medicine, Animals, Transferase, Molecular Biology, Polymerase, Antibody, ADP Ribose Transferases, chemistry.chemical_classification, Adenosine Diphosphate Ribose, biology, medicine.diagnostic_test, ved/biology, Thermophile, Sulfolobus solfataricus, Cell Biology, biology.organism_classification, Immunohistochemistry, Molecular biology, Archaea, Molecular Weight, Enzyme, chemistry, Polyclonal antibodies, biology.protein, Cattle, Poly(ADP-ribose) Polymerases, ADP-ribosylation
Abstract

Polyclonal antibodies raised against eukaryotic mono(ADPribose)transferase and poly(ADPribose)polymerase were used to test the presence of antigenic determinants in a crude extract of Sulfolobus solfataricus, a thermophilic archaeon. Samples from eukaryotic (bull testis) and bacterial (E. coli) sources were analysed for comparison. All tested antibodies reacted with the sulfolobal sample with a specificity comparable to that of the eukaryotic preparation, as revealed by ELISA test, activity assays in the presence of antibodies and immunoblot experiments. After electrophoresis and western blot of sulfolobal proteins, a band at a mass around 50 kDa was detected by immunostaining.

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