Home |  English version |  Mappa |  Commenti |  Sondaggio |  Staff |  Contattaci Cerca nel sito  
Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2007

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Molecular adaptation strategies to high temperature and thermal denaturation mechanism of the D-trehalose/D-maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis

Anno di pubblicazione: 2007

Formato: Elettronico

Autori: Fessas D.; Staiano M.; Barbiroli A.; Marabotti A.; Schiraldi A.; Varriale A.; Rossi M.; D'Auria S.

Affiliazioni autori: Department of Food Science, Technology and Microbiology, University of Milan, Milan, Italy Istituto di Biochimica delle Proteine, CNR, Napoli, Italy Laboratorio di Bioinformatica, Istituto di Scienze dell'Alimentazione, CNR, Avellino, Italy

Autori CNR:


Lingua: inglese

Abstract: The D-trehalose/D-maltose-binding protein (TMBP), a monomeric protein of 48 kDa, is one component of the trehalose and maltose uptake system. In the hyperthermophilic archaeon T. litoralis this is mediated by a protein-dependent ATPbinding cassette system transporter. The gene coding for a thermostable TMBP from the archaeon T. litoralis has been cloned, and the recombinant protein has been expressed in E. coli. The recombinant TMBP has been purified to homogeneity and characterized. It exhibits the same functional and structural properties as the native one. In fact, it is highly thermostable and binds both trehalose and maltose with high affinity. In this work we used differential scanning calorimetry studies together with a detailed analysis, at the molecular level, of the three-dimensional protein structure to shed light on the basis of the high thermostability exhibited by the recombinant TMBP from the archaeon T. litoralis. The obtained data suggest that the presence of trehalose does not change the overall mechanism of the denaturation of this protein but it selectively modifies the stability of the TMBP structural domains.

Lingua abstract: inglese

Pagine da: 1002

Pagine a: 1009


Proteins Alan R. Liss,
Paese di pubblicazione: Stati Uniti d'America
Lingua: inglese
ISSN: 0887-3585

Numero volume: 67

Numero fascicolo: 4

DOI: 10.1002/prot.21383

Referee: Sė: Internazionale

Indicizzato da: ISI Web of Science (WOS) [000246415700020]

Parole chiave:


Strutture CNR:


Torna indietro Richiedi modifiche Invia per email Stampa
Home Il CNR  |  I servizi News |   Eventi | Istituti |  Focus