Zinc(II) Complexes of Ubiquitin: Speciation, Affinity and Binding Features (Articolo in rivista)

Type
Label
  • Zinc(II) Complexes of Ubiquitin: Speciation, Affinity and Binding Features (Articolo in rivista) (literal)
Anno
  • 2011-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/chem.201101364 (literal)
Alternative label
  • G Arena, R Fattorusso, G Grasso, G I Grasso, C Isernia, G Malgieri, Milardi D, * E Rizzarelli (2011)
    Zinc(II) Complexes of Ubiquitin: Speciation, Affinity and Binding Features
    in Chemistry - A European Journal; Wiley-VCH Verlag Gmbh, Weinheim (Germania)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • G Arena, R Fattorusso, G Grasso, G I Grasso, C Isernia, G Malgieri, Milardi D, * E Rizzarelli (literal)
Pagina inizio
  • 11596 (literal)
Pagina fine
  • 11603 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 17 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 8 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 41 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • D. Milardi, Istituto di Biostrutture e Bioimmagini-UOS CT, Consiglio Nazionale delle Ricerche, V.le A. Doria 6, 95125 Catania (Italy). G. Arena, G. Grasso, G. I. Grasso, E. Rizzarelli, Dipartimento di Scienze Chimiche, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania (Italy). R. Fattorusso, C. Isernia, Dr. G. Malgieri, Dipartimento di Scienze Ambientali, Seconda Università di Napoli, Via A.Vivaldi 43, 81100, Caserta (Italy). (literal)
Titolo
  • Zinc(II) Complexes of Ubiquitin: Speciation, Affinity and Binding Features (literal)
Abstract
  • Intraneuronal inclusions consisting of hypermetallated, (poly-)ubiquitinated proteins are a hallmark of neurodegeneration. To highlight the possible role played by metal ions in the dysfunction of the ubiquitin-proteasome system, here we report on zinc(II)/ubiquitin binding in terms of affinity constants, speciation, preferential binding sites and effects on protein stability and self-assembly. Potentiometric titrations allowed us to establish that at neutral pH only two species, ZnUb and Zn2Ub, are present in solution, in line with ESI-MS data. A change in the diffusion coefficient of ubiquitin was observed by NMR DOSY experiments after addition of ZnII ions, and thus indicates metal-promoted formation of protein assemblies. Analysis of 1H, 15N, 13C? and 13CO chemical-shift perturbation after equimolar addition of ZnII ions to ubiquitin outlined two different metal-binding modes. The first involves a dynamic equilibrium in which zinc(II) is shared between a region including Met1, Gln2, Ile3, Phe4, Thr12, Leu15, Glu16, Val17, Glu18, Ile61 and Gln62 residues, which represent a site already described for copper binding, and a domain comprising Ile23, Glu24, Lys27, Ala28, Gln49, Glu51, Asp52, Arg54 and Thr55 residues. A second looser binding mode is centred on His68. Differential scanning calorimetry evidenced that addition of increasing amounts of ZnII ions does not affect protein thermal stability; rather it influences the shape of thermograms because of the increased propensity of ubiquitin to self-associate. The results presented here indicate that ZnII ions may interact with specific regions of ubiquitin and promote protein-protein contacts. (literal)
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