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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: Homology-Based Modeling of Universal Stress Protein from Listeria innocua Up-Regulated under Acid Stress Conditions

Anno di pubblicazione: 2016

Autori: Tremonte, Patrizio; Succi, Mariantonietta; Coppola, Raffaele; Sorrentino, Elena; Tipaldi, Luca; Picariello, Gianluca; Pannella, Gianfranco; Fraternali, Franca

Affiliazioni autori: Univ Molise; Natl Res Council ISA CNR; New Hunts House Kings Coll

Autori CNR:


Lingua: inglese

Abstract: An Universal Stress Protein (USP) expressed under acid stress condition by Listeria innocua ATCC 33090 was investigated. The USP was up-regulated not only in the stationary phase but also during the exponential growth phase. The three dimensional (3D) structure of USP was predicted using a combined proteomic and bioinformatics approach. Phylogenetic analysis showed that the USP from Listeria detected in our study was distant from the USPs of other bacteria (such as Pseudomonas spp., Escherichia coil, Salmonella spp.) and clustered in a separate and heterogeneous class including several USPs from Listeria spp. and Lactobacillus spp. An important information on the studied USP was obtained from the 3D-structure established through the homology modeling procedure. In detail, the Model_USP-691 suggested that the investigated USP had a homo-tetrameric quaternary structure. Each monomer presented an architecture analogous to the Rossmann-like alpha/beta-fold with five parallel beta-strands, and four alpha-helices. The analysis of monomer-monomer interfaces and quality of the structure alignments confirmed the model reliability. In fact, the structurally and sequentially conserved hydrophobic residues of the beta t-strand 5 (in particular the residues V-146 and V-148) were involved in the inter-chains contact. Moreover, the highly conserved residues 1139 and H-141 in the region alpha 4 were involved in the dimer association and functioned as hot spots into monomer monomer interface assembly. The hypothetical assembly of dimers was also supported by the large interface area and by the negative value of solvation free energy gain upon interface interaction. Finally, the structurally conserved ATP-binding motif G-2X-G-9X-G(S/T-N) suggested for a putative role of ATP in stabilizing the tetrameric assembly of the USP. Therefore, the results obtained from a multiple approach, consisting in the application of kinetic, proteomic, phylogenetic and modeling analyses, suggest that Listeria USP could be considered a new type of ATP-binding USP involved in the response to acid stress condition during the exponential growth phase.

Lingua abstract: inglese

Pagine totali: 17


Frontiers in microbiology Frontiers Research Foundation,
Paese di pubblicazione: Svizzera
Lingua: inglese
ISSN: 1664-302X

Numero volume: 7

DOI: 10.3389/fmicb.2016.01998

Referee: Sė: Internazionale

Stato della pubblicazione: Published version

Indicizzato da: ISI Web of Science (WOS) [000390158000001]

Parole chiave:

  • universal stress protein
  • acid stress
  • Listeria
  • exponential growth phase
  • homology modeling
  • 2-D Electrophoresis
  • ATP-binding motif

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