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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2016

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Proline 235 plays a key role in the regulation of the oligomeric states of Thermotoga maritima Arginine Binding Protein

Anno di pubblicazione: 2016

Autori: Smaldone, Giovanni; Vigorita, Marilisa; Ruggiero, Alessia; Balasco, Nicole; Dattelbaum, Jonathan D.; D'Auria, Sabato; Del Vecchio, Pompea; Graziano, Giuseppe; Vitagliano, Luigi

Affiliazioni autori: IRCCS SDN; Univ Sannio; CNR; Univ Naples 2; Univ Richmond; CNR; Univ Naples Federico II

Autori CNR:

  • SABATO D'AURIA

Lingua: inglese

Abstract: The Arginine Binding Protein isolated from Thermotoga maritima (TmArgBP) is a protein endowed with several peculiar properties. We have previously shown that TmArgBP dimerization is a consequence of the swapping of the C-terminal helix. Here we explored the structural determinants of TmArgBP domain swapping and oligomerization. In particular, we report a mutational analysis of the residue Pro235, which is located in the hinge region of the swapping dimer. This residue was either replaced with a Gly-Lys dipeptide (TmArgBP(P235GK)) or a Gly residue (TmArgBP(P235G)).

Lingua abstract: inglese

Altro abstract: Different forms of these mutants were generated and extensively characterized using biophysical techniques. For both TmArgBP(P235GK) and TmArgBP(P235G) mutants, the occurrence of multiple oligomerization states (monomers, dimers and trimers) was detected. The formation of well-folded monomeric forms for these mutants indicates that the dimerization through C-terminal domain swapping observed in wild-type TmArgBP is driven by conformational restraints imposed by the presence of Pro235 in the hinge region. Molecular dynamics studies corroborate this observation by showing that Gly235 assumes conformational states forbidden for Pro residues in the TmArgBPP235G monomer. Unexpectedly, the trimeric forms present: (a) peculiar circular dichroism spectra, (b) a great susceptibility to heating, and (c) the ability to bind the Thioflavin T dye.

Pagine da: 814

Pagine a: 824

Pagine totali: 11

Rivista:

Biochimica et biophysica acta. Proteins and proteomics Elsevier
Paese di pubblicazione: Paesi Bassi
Lingua: inglese
ISSN: 1570-9639

Numero volume: 1864

Numero fascicolo: 7

DOI: 10.1016/j.bbapap.2016.04.006

Stato della pubblicazione: Published version

Indicizzato da: ISI Web of Science (WOS) [000376706900008]

Parole chiave:

  • Domain swapping
  • Protein oligomerization
  • Protein structure dynamics
  • Protein structure-stability
  • Differential scanning calorimetry

Strutture CNR:

 
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