http://www.cnr.it/ontology/cnr/individuo/prodotto/ID14953
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)
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- 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
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- Gentile F., Amodeo P., Febbraio F., Picaro F., Motta A. Formisano S., Nucci R. (literal)
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- 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)
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- 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)
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- ISI Web of Science (WOS) (literal)
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- 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.
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