SDS-resistant Active and Thermostable Dimers Are Obtained from the Dissociation of Homotetrameric b-glycosidase From Hyperthermophilic Sulfolobus Solfataricus in SDS. Stabilizing Role of the A-C Intermonomeric Interface (Articolo in rivista)

Type
Label
  • SDS-resistant Active and Thermostable Dimers Are Obtained from the Dissociation of Homotetrameric b-glycosidase From Hyperthermophilic Sulfolobus Solfataricus in SDS. Stabilizing Role of the A-C Intermonomeric Interface (Articolo in rivista) (literal)
Anno
  • 2002-01-01T00:00:00+01:00 (literal)
Alternative label
  • Gentile F., Amodeo P., Febbraio F., Picaro F., Motta A. Formisano S., Nucci R. (2002)
    SDS-resistant Active and Thermostable Dimers Are Obtained from the Dissociation of Homotetrameric b-glycosidase From Hyperthermophilic Sulfolobus Solfataricus in SDS. Stabilizing Role of the A-C Intermonomeric Interface
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Gentile F., Amodeo P., Febbraio F., Picaro F., Motta A. Formisano S., Nucci R. (literal)
Pagina inizio
  • 44050 (literal)
Pagina fine
  • 44060 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • La comprensione dei meccanismi di resistenza alla dissociazione mediante SDS può essere utile nella comprensione degli stessi meccanismi osservati in sistemi proteici coinvolti nella presentazioni di antigeni alle cellule del sistema immunitario e in importanti patologie neurodegenerative quali l'Alzheimer. (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 277 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • Questo lavoro descrive gli effetti del sodio dodecilsolfato (SDS) sulla struttura quaternaria della beta-glicosidasi. In presenza di SDS il tetramero si dissocia in dimeri che conservano molta della loro attività biologica. Ciò è dovuto alla presenza di un network di interazioni polari presenti all'interfaccia dei dimeri. (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • F. Gentile, F. Picaro, S. Formisano: IEOS, CNR; P. Amodeo, A. Motta: ICB, CNR; F. Febbraio, R. Nucci: IBP, CNR. (literal)
Titolo
  • SDS-resistant Active and Thermostable Dimers Are Obtained from the Dissociation of Homotetrameric b-glycosidase From Hyperthermophilic Sulfolobus Solfataricus in SDS. Stabilizing Role of the A-C Intermonomeric Interface (literal)
Abstract
  • beta-Glycosidases are fundamental, widely conserved enzymes. Those from hyperthermophiles exhibit unusual stabilities toward various perturbants. Previous work with homotetrameric beta-glycosidase from hyperthermophilic Sulfolobus solfataricus (M(r) 226,760) has shown that addition of 0.05- 0.1% SDS was associated with minimal secondary structure perturbations and increased activity. This work addresses the effects of SDS on beta-glycosidase quaternary structure. In 0.1-1% SDS, the enzyme was dimeric, as determined by Ferguson analysis of transverse-gradient polyacrylamide gels. The catalytic activity of the beta-glycosidase dimer in SDS was determined by in-gel assay. A minor decrease of thermal stability in SDS was observed after exposure to temperatures up to 80 degrees C for 1 h. An analysis of beta-glycosidase crystal structure showed different changes in solvent-accessible surface area on going from the tetramer to the two possible dimers (A-C and A-D). Energy minimization and molecular dynamics calculations showed that the A-C dimer, exhibiting the lowest exposed surface area, was more stabilized by a network of polar interactions. The charge distribution around the A-C interface was characterized by a local short range anisotropy, resulting in an unfavorable interaction with SDS. This paper provides a detailed description of an SDS-resistant inter-monomeric interface, which may help understand similar interfaces involved in important biological processes. (literal)
Prodotto di
Autore CNR
Insieme di parole chiave

Incoming links:


Autore CNR di
Prodotto
Insieme di parole chiave di
data.CNR.it