http://www.cnr.it/ontology/cnr/individuo/prodotto/ID13351
The Arabidopsis SUPERMAN protein is able to specifically bind DNA through its single Cys2-His2 zinc finger motif (Articolo in rivista)
- Type
- Label
- The Arabidopsis SUPERMAN protein is able to specifically bind DNA through its single Cys2-His2 zinc finger motif (Articolo in rivista) (literal)
- Anno
- 2002-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1093/nar/gk613 (literal)
- Alternative label
Dathan N., Zaccaro L., Esposito S., Isernia C., Omichinski J G., Riccio A, Pedone C., Di Blasio B., Fattorusso R., Pedone P. V. (2002)
The Arabidopsis SUPERMAN protein is able to specifically bind DNA through its single Cys2-His2 zinc finger motif
in Nucleic acids research
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Dathan N., Zaccaro L., Esposito S., Isernia C., Omichinski J G., Riccio A, Pedone C., Di Blasio B., Fattorusso R., Pedone P. V. (literal)
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- Pagina fine
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- Rivista
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- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Biostrutture e Bioimmagini, Via Mezzocannone 6, 80134 Napoli, Italy
Département de Biochimie, Université de Montréal, Montréal, Quebec, Canada. (literal)
- Titolo
- The Arabidopsis SUPERMAN protein is able to specifically bind DNA through its single Cys2-His2 zinc finger motif (literal)
- Abstract
- The Arabidopsis SUPERMAN (SUP) gene has been shown to be important in
maintaining the boundary between stamens and carpels, and is presumed to
act by regulating cell proliferation. In this work, we show that the SUP
protein, which contains a single Cys2-His2 zinc finger domain including the
QALGGH sequence, highly conserved in the plant zinc finger proteins, binds
DNA. Using a series of deletion mutants, it was detd. that the minimal
domain required for specific DNA binding (residues 15-78) includes the
single zinc finger and two basic regions located on either side of this
motif. Furthermore, amino acid substitutions in the zinc finger or in the
basic regions, including a mutation that knocks out the function of the SUP
protein in vivo (glycine 63 to aspartate), have been found to abolish the
activity of the SUP DNA-binding domain. These results strongly suggest
that the SUP protein functions in vivo by acting as a DNA-binding protein,
likely involved in transcriptional regulation. The assocn. of both an
N-terminal and a C-terminal basic region with a single Cys2-His2 zinc
finger represents a novel DNA-binding motif suggesting that the mechanism
of DNA recognition adopted by the SUP protein is different from that
described so far in other zinc finger proteins. (literal)
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