Thermal and chemical stability of two homologous POZ/BTB domains of KCTD proteins characterized by a different oligomeric organization(486 views) Pirone L, Esposito C, Correale S, Graziano G, Di Gaetano S, Vitagliano L, Pedone E
Biomed Res Int (ISSN: 2314-6133, 2314-6141, 2314-6141electronic), 2013; 2013: 162674-162674.
Keywords: Btb Protein, Histone Deacetylase 1, Kctd Protein, Poz Protein, Tetramer, Unclassified Drug, Kcash3 Protein, Human, Kctd5 Protein, Potassium Channel, Signal Transducing Adaptor Protein, Urea, Article, Degradation, Denaturation, Protein Secondary Structure, Thermostability, Ubiquitination, Chemistry, Circular Dichroism, Light, Protein Denaturation, Protein Multimerization, Protein Stability, Protein Tertiary Structure, Radiation Scattering, Sequence Analysis, Sequence Homology, Spectrofluorometry, Temperature, Protein Structure, Amino Acid, Spectrometry, Fluorescence, Pharmacology,
Affiliations: *** IBB - CNR ***
Istituto di Cristallografia, CNR, Via G. Amendola 122/O, 70126 Bari, Italy
DFM Scarl, Via Mezzocannone 16, 80134 Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Napoli, Italy
Kedrion S.p.A, S. Antimo, 80029 Napoli, Italy
Dipartimento di Scienze per la Biologia, la Geologia e l'Ambiente, Università Del Sannio, Via Port'Arsa 11, 82100 Benevento, Italy
Kedrion S. p. A, S. Antimo, 80029 Napoli, Italy
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Thermal and chemical stability of two homologous POZ/BTB domains of KCTD proteins characterized by a different oligomeric organization
POZ/BTB domains are widespread modules detected in a variety of different biological contexts. Here, we report a biophysical characterization of the POZ/BTB of KCTD6, a protein that is involved in the turnover of the muscle small ankyrin-1 isoform 5 and, in combination with KCTD11, in the ubiquitination and degradation of HDAC1. The analyses show that the domain is a tetramer made up by subunits with the expected alpha /beta structure. A detailed investigation of its stability, carried out in comparison with the homologous pentameric POZ/BTB domain isolated from KCTD5, highlights a number of interesting features, which are shared by the two domains despite their different organization. Their thermal/chemical denaturation curves are characterized by a single and sharp inflection point, suggesting that the denaturation of the two domains is a cooperative two-state process. Furthermore, both domains present a significant content of secondary structure in their denatured state and a reversible denaturation process. We suggest that the ability of these domains to fold and unfold reversibly, a property that is somewhat unexpected for these oligomeric assemblies, may have important implications for their biological function. Indeed, these properties likely favor the formation of heteromeric associations that may be essential for the intricate regulation of the processes in which these proteins are involved.
Thermal and chemical stability of two homologous POZ/BTB domains of KCTD proteins characterized by a different oligomeric organization
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(288 views) Oncotarget (ISSN: 1949-2553electronic, 1949-2553linking), 2018 May 22; 9(39): 25630-25646. Impact Factor:5.008 ViewExport to BibTeXExport to EndNote