PNA zipper as a dimerization tool: development of a bZip mimic (Articolo in rivista)

Type
Label
  • PNA zipper as a dimerization tool: development of a bZip mimic (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/bip.21357 (literal)
Alternative label
  • Pensato S, Renda M, Leccia F, Saviano M, D'Andrea LD, Pedone C, Pedone PV, Romanelli A (2010)
    PNA zipper as a dimerization tool: development of a bZip mimic
    in Biopolymers (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Pensato S, Renda M, Leccia F, Saviano M, D'Andrea LD, Pedone C, Pedone PV, Romanelli A (literal)
Pagina inizio
  • 434 (literal)
Pagina fine
  • 441 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 93 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Pensato S, CNR, Inst Biostruct & Bioimaging, I-80125 Naples, Italy Renda M, Univ Naples 2, Dept Environm Sci, Caserta, Italy Leccia F, Univ Naples 2, Dept Environm Sci, Caserta, Italy Saviano M, CNR, Inst Biostruct & Bioimaging, I-80125 Naples, Italy D'Andrea LD, CNR, Inst Biostruct & Bioimaging, I-80125 Naples, Italy Pedone C, Univ Naples Federico 2, Dept Biol Sci, Sch Biotechnol Sci, Naples, Italy Pedone PV, Univ Naples 2, Dept Environm Sci, Caserta, Italy Romanelli A,Univ Naples Federico 2, Dept Biol Sci, Sch Biotechnol Sci, Naples, Italy (literal)
Titolo
  • PNA zipper as a dimerization tool: development of a bZip mimic (literal)
Abstract
  • The article describes the use of a PNA duplex (PNA zipper) as a tool to dimerize or bring in close proximity two polypeptides or protein domains. The amino acid sequence to be dimerized is covalently bound to complementary PNA sequences. Annealing of the PNA strands results in dimer formation. To test the ability of the \"PNA-zipper\" as a dimerization tool, we designed a GCN4 mimetic, where the leucine-zipper dimerization domain was replaced by the PNA zipper, whereas the basic DNA-binding domain was covalently attached to the PNA. The molecule was assembled by chemical ligation of the peptide corresponding to the DNA-binding domain of GCN4 modified with a succinyl thioester with two complementary PNAs harboring a cysteine residue. Electromobility-shift experiments show the ability of the PNA zipper-GCN4 to bind selected DNA duplexes. The PNA zipper-GCN4 binds both the TRE and CRE DNA sites, but it does not bind TRE and C RE mutants containing even a single base mutation, as the native GCN4. The ability to fold upon complexation with DNA was investigated by CD. A good correlation between the ability of the PNA zipper-GCN4 to fold into a helices and the ability to hind DNA was found (literal)
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