DNA-binding specificity of the homeodomain leucine zipper domain (Articolo in rivista)

Type
Label
  • DNA-binding specificity of the homeodomain leucine zipper domain (Articolo in rivista) (literal)
Anno
  • 1997-01-01T00:00:00+01:00 (literal)
Alternative label
  • G Sessa (1); G Morelli (2); Ruberti I (1) (1997)
    DNA-binding specificity of the homeodomain leucine zipper domain
    in Journal of Molecular Biology; ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD, LONDON (Regno Unito)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • G Sessa (1); G Morelli (2); Ruberti I (1) (literal)
Pagina inizio
  • 303 (literal)
Pagina fine
  • 309 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 274 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 3 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • (1) Istituto di Biologia e Patologia Molecolari (2) Istituto di Ricerca per la Nutrizione e gli Alimenti (literal)
Titolo
  • DNA-binding specificity of the homeodomain leucine zipper domain (literal)
Abstract
  • Homeodomain-leucine zipper (HD-Zip) proteins are putative transcription factors identified only in plants. The study of the DNA-binding properties of the ATHB-1 and -2 HD-Zip (HD-Zip-l and -2) domains showed that they interact with DNA as homodimers and recognize two distinct 9 bp pseudopalindromic sequences, CAAT(A/T)ATTG (BS-1) and CAAT(G/C)ATTG (BS-2), respectively, as determined by selecting high-affinity binding sites from random-sequence DNA. Here, we report a mutational analysis of the HD-Zip-2 domain. We determined that conserved amino acid residues of helix 3, Val47 and Asn51, and Arg55 are essential for the DNA-binding activity of the HD-Zip-2 domain. We demonstrated that the preferential recognition of a G/C base-pair at the central position by the HD-Zip-2 domain is abolished either by the replacement of Arg55 with lysine or by the substitution of Glu46 and Thr56 with the corresponding residues of the HD-Zip-l domain (alanine and tryptophan, respectively). In contrast, substitution of Arg55 with lysine in the HD-Zip-3 domain significantly reduced DNA-binding activity without changing the specificity of recognition. Finally, we determined that differences in residues outside helix 3 further contribute to the DNA-binding specificity of the HD-Zip domain. Taken together, the data strongly suggest that the preferential recognition of BS-2 and -1 by the HD-Zip-2 and -1, domains, respectively, may be attributable to a distinct orientation of the side-chain of Arg55 in these two domains. (literal)
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