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

Torna all'elenco Contributi in rivista anno 2006

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Structure/function of KRAB repression domains: Structural properties of KRAB modules inferred from hydrodynamic, circular dichroism, and FTIR spectroscopic analyses

Anno di pubblicazione: 2006

Formato: Elettronico

Autori: Riccardo Mannini 1; Vincenzo Rivieccio 1; Sabato D'Auria 2; Fabio Tanfani 3; Alessio Ausili 3; Aangelo Facchiano 4; Carlo Pedone 5; Giovanna Grimaldi 1

Affiliazioni autori: 1 CNR - Istituto di Genetica e Biofisica Adriano Buzzati-Traverso, Italy 2 CNR - Istituto di Biochimica delle Proteine,Italy 3 UniversitÓ Politecnica delle Marche. Istituto di Biochimica, Italy 4 CNR - Istituto di Scienze dell'Alimentazione, Italy 5 CNR - Istituto di Biostrutture e Bioimmagini, Italy

Autori CNR:

  • SABATO D'AURIA
  • ANGELO FACCHIANO
  • GIOVANNA GRIMALDI
  • CARLO PEDONE

Lingua: inglese

Abstract: The abundant zinc finger proteins (ZFPs) sharing the KRAB motif, a potent transcription repression domain, direct the assembly on templates of multiprotein repression complexes. A pivotal step in this pathway is the assembly of a KRAB domain-directed complex with a primary corepressor, KAP1/KRIP-1/TIF1. The structure/function dependence of KRAB/TIF1 protein-protein interaction and properties of the complex, therefore, play pivotal roles in diverse cellular processes depending on KRAB-ZFPs regulation. KRAB domains are functionally bipartite. The 42 amino acid-long KRAB-A module, indeed, is necessary and sufficient for transcriptional repression and for the interaction with the tripartite RBCC region of TIF1, while the KRAB-B motif seems to potentiate the assembly of the complex. The structural properties of KRAB-A and KRAB-AB domains from the human ZNF2 protein have been investigated by characterizing highly purified lone (A) and composite (AB) modules. Hydrodynamic and spectroscopic features, investigated by means of gel filtration, circular dichroism, and infrared spectroscopy, provide evidence that both KRAB-A and KRAB-AB domains present low compactness, structural disorder, residual secondary structure content, flexibility, and tendency to molecular aggregation. Comparative analysis among KRAB-A and KRAB-AB modules suggests that the presence of the -B module may influence the properties of lone KRAB-A by affecting the structural flexibility and stability of the conformers. The combined experimental data and the intrinsic features of KRAB-A and KRAB-AB primary structures indicate a potential role of specific subregions within the modules in driving structural flexibility, which is proposed to be of importance for their function.

Lingua abstract: inglese

Pagine da: 604

Pagine a: 616

Rivista:

Proteins John Wiley & Sons
Paese di pubblicazione: Stati Uniti d'America
Lingua: inglese
ISSN: 1097-0134

Numero volume: 62

Numero fascicolo: 3

DOI: 10.1002/prot.20792

Indicizzato da: ISI Web of Science (WOS) [000235172100005]

Parole chiave:

  • circular dichroism
  • FTIR
  • KRAB
  • structural content

Strutture CNR:

Moduli:

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