Homeotic proteins participate in the function of human-DNA replication origins. (Articolo in rivista)

Type
Label
  • Homeotic proteins participate in the function of human-DNA replication origins. (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1093/nar/gkq688 (literal)
Alternative label
  • Marchetti L; Comelli L; D'Innocenzo B; Puzzi L; Luin S; Arosio D; Calvello M; Mendoza-Maldonado R; Peverali F; Trovato F; Riva S; Biamonti G; Abdurashidova G; Beltram F; Falaschi A. (2010)
    Homeotic proteins participate in the function of human-DNA replication origins.
    in Nucleic acids research; Oxford University Press, Oxford (Regno Unito)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Marchetti L; Comelli L; D'Innocenzo B; Puzzi L; Luin S; Arosio D; Calvello M; Mendoza-Maldonado R; Peverali F; Trovato F; Riva S; Biamonti G; Abdurashidova G; Beltram F; Falaschi A. (literal)
Pagina inizio
  • 8105 (literal)
Pagina fine
  • 8119 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://nar.oxfordjournals.org/content/38/22/8105.full (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 38 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 22 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
  • PubMe (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • NEST, Scuola Normale Superiore and Istituto Nanoscienze-CNR, Laboratorio di Biologia Molecolare, Scuola Normale Superiore, Pisa, Istituto di Biofisica-CNR, Trento Povo, International Centre for Genetic Engineering and Biotechnology, Trieste, Istituto di Genetica Molecolare-CNR, Pavia, IIT-NEST, Center for Nanotechnology Innovation, Pisa and Istituto di Fisiologia Clinica-CNR, Pisa, Italy. (literal)
Titolo
  • Homeotic proteins participate in the function of human-DNA replication origins. (literal)
Abstract
  • Recent evidence points to homeotic proteins as actors in the crosstalk between development and DNA replication. The present work demonstrates that HOXC13, previously identified as a new member of human DNA replicative complexes, is a stable component of early replicating chromatin in living cells: it displays a slow nuclear dynamics due to its anchoring to the DNA minor groove via the arginine-5 residue of the homeodomain. HOXC13 binds in vivo to the lamin B2 origin in a cell-cycle-dependent manner consistent with origin function; the interaction maps with nucleotide precision within the replicative complex. HOXC13 displays in vitro affinity for other replicative complex proteins; it interacts also in vivo with the same proteins in a cell-cycle-dependent fashion. Chromatin-structure modifying treatments, disturbing origin function, reduce also HOXC13–origin interaction. The described interactions are not restricted to a single origin nor to a single homeotic protein (also HOXC10 binds the lamin B2 origin in vivo). Thus, HOX complexes probably contribute in a general, structure-dependent manner, to origin identification and assembly of replicative complexes thereon, in presence of specific chromatin configurations. (literal)
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