Thermal stability and aggregation of Sulfolobus solfataricus beta-glycosidase are dependent upon N-epsilon-methylation of specific lysyl residues (Articolo in rivista)

Type
Label
  • Thermal stability and aggregation of Sulfolobus solfataricus beta-glycosidase are dependent upon N-epsilon-methylation of specific lysyl residues (Articolo in rivista) (literal)
Anno
  • 2004-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1074/jbc.M308520200 (literal)
Alternative label
  • Febbraio F; Andolfo A; Tanfani F; Briante R; Gentile F; Formisano S; Vaccaro C; Scire A; Bertoli E; Pucci P; Nucci R. (2004)
    Thermal stability and aggregation of Sulfolobus solfataricus beta-glycosidase are dependent upon N-epsilon-methylation of specific lysyl residues
    in The Journal of biological chemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Febbraio F; Andolfo A; Tanfani F; Briante R; Gentile F; Formisano S; Vaccaro C; Scire A; Bertoli E; Pucci P; Nucci R. (literal)
Pagina inizio
  • 10185 (literal)
Pagina fine
  • 10194 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 279 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 11 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Protein Biochemistry, CNR, Via Marconi 10, 80125 Napoli, Italy, CEINGE Advanced Biotechnologies scarl, Via Pansini 5, 80131 Napoli, Italy, and Department of Organic and Biological Chemistry, University of Naples \"Federico II,\" Via Cinthia, 80126 Napoli, Italy Institute of Biochemistry, Faculty of Medicine and Surgery, and Faculty of Sciences, Polytechnical University of Marche, Via Ranieri, 60131 Ancona, Italy, Department SAVA, University of Molise, Via De Sanctis, 86100 Campobasso, Italy, Department of Cell and Molecular Biology and Pathology, University of Naples \"Federico II\" and Institute of Experimental Endocrinology and Oncology, CNR, Via Pansini 5, 80131 Napoli, Italy, (literal)
Titolo
  • Thermal stability and aggregation of Sulfolobus solfataricus beta-glycosidase are dependent upon N-epsilon-methylation of specific lysyl residues (literal)
Abstract
  • Methylation in vivo is a post-translational modification observed in several organisms belonging to Eucarya, Bacteria and Archaea. Although important implications of this modification have been demonstrated in several eucaryotes, its biological role in hyperthermophilic Archaea is far to be understood. The aim of this work is to clarify some effects of methylation on the properties of beta-glycosidase from Sulfolobus solfataricus, by a structural comparison between the native, methylated protein and its unmethylated counterpart, recombinantly expressed in E. coli. Analysis by FT-IR spectroscopy indicated similar secondary structure contents for the two forms of the protein. However, the study of temperature perturbation by FT-IR spectroscopy and turbidimetry evidenced denaturation and aggregation events more pronounced in recombinant than in native beta-glycosidase. Red nile fluorescence analysis revealed significant differences of surface hydrophobicity between the two forms of the protein. Unlike the native enzyme, which dissociated into SDS-resistant dimers upon exposure to the detergent, the recombinant enzyme partially dissociated into monomers. By electrospray mapping, the methylation sites of the native protein were identified. A computational analysis of beta-glycosidase three-dimensional structure, and comparisons with other proteins from S. solfataricus revealed analogies in the localization of methylation sites in terms of secondary structural elements and overall topology. These observations suggest a role for the methylation of lysyl residues, located in selected domains, in the thermal stabilization of beta-glycosidase from S. solfataricus. (literal)
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