Structural and functional studies of Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx: a novel peculiar member of the winged helix-turn-helix transcription factor family
Structural and functional studies of Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx: a novel peculiar member of the winged helix-turn-helix transcription factor family(521 views) Contursi P, Farina B, Pirone L, Fusco S, Russo L, Bartolucci S, Fattorusso R, Pedone E
Nucleic Acids Res (ISSN: 0305-1048, 1362-4962), 2014; 42(9): 5993-6011.
Keywords: Bacterial Protein, Dna, Helix Loop Helix Protein, Protein Stf76, Recombinant Protein, Unclassified Drug, Amino Acid Composition, Article, Circular Dichroism, Computer Program, Controlled Study, Dna Protein Complex, Dna Template, Escherichia Coli, Gene Expression Regulation, Isothermal Titration Calorimetry, Light Scattering, Molecular Recognition, Nuclear Magnetic Resonance, Nucleotide Binding Site, Open Reading Frame, Plasmid, Priority Journal, Promoter Region, Sequence Homology, Spectrofluorometry, Structure Activity Relation, Sulfolobus, Sulfolobus Islandicus, Three Dimensional Imaging, Virus Strain, Amino Acid Sequence, Base Sequence, Fuselloviridae, Models, Molecular Sequence Data, Biomolecular, Protein Binding, Protein Structure, Quaternary, Secondary, Solutions, Viral Proteins, Winged-Helix Transcription Factors,
Affiliations: *** IBB - CNR ***
Dipartimento di Biologia, Università degli Studi di Napoli Federico II, Napoli 80126, Italy
Interuniversity Centre for Research on Bioactive Peptides (CIRPEB), University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy
Istituto di Cristallografia, C.N.R., Bari 70126, Italy
Dipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Seconda Università di Napoli, Caserta 81100, Italy
Istituto di Biostrutture e Bioimmagini, C.N.R., Napoli 80134, Italy
References: Not available.
Structural and functional studies of Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx: a novel peculiar member of the winged helix-turn-helix transcription factor family
The hybrid plasmid-virus pSSVx from Sulfolobus islandicus presents an open reading frame encoding a 76 amino acid protein, namely Stf76, that does not show significant sequence homology with any protein with known 3D structure. The recombinant protein recognizes specifically two DNA-binding sites located in its own promoter, thus suggesting an auto-regulated role of its expression. Circular dichroism, spectrofluorimetric, light scattering and isothermal titration calorimetry experiments indicated a 2:1 molar ratio (protein:DNA) upon binding to the DNA target containing a single site. Furthermore, the solution structure of Stf76, determined by nuclear magnetic resonance (NMR) using chemical shift Rosetta software, has shown that the protein assumes a winged helix-turn-helix fold. NMR chemical shift perturbation analysis has been performed for the identification of the residues responsible for DNA interaction. In addition, a model of the Stf76-DNA complex has been built using as template a structurally related homolog.
Structural and functional studies of Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx: a novel peculiar member of the winged helix-turn-helix transcription factor family
Structural and functional studies of Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx: a novel peculiar member of the winged helix-turn-helix transcription factor family
Petraglia F, Singh AA, Carafa V, Nebbioso A, Conte M, Scisciola L, Valente S, Baldi A, Mandoli A, Petrizzi VB, Ingenito C, De Falco S, Cicatiello V, Apicella I, Janssen-megens EM, Kim B, Yi G, Logie C, Heath S, Ruvo M, Wierenga ATJ, Flicek P, Yaspo ML, Della Valle V, Bernard O, Tomassi S, Novellino E, Feoli A, Sbardella G, Gut I, Vellenga E, Stunnenberg HG, Mai A, Martens JHA, Altucci L * Combined HAT/EZH2 modulation leads to cancer-selective cell death(452 views) Oncotarget (ISSN: 1949-2553electronic, 1949-2553linking), 2018 May 22; 9(39): 25630-25646. Impact Factor:5.008 ViewExport to BibTeXExport to EndNote