Nucleic Acids Research, 2002, Vol. 30, No. 22 4945-4951
© 2002 Oxford University Press
The Arabidopsis SUPERMAN protein is able to specifically bind DNA through its single Cys2–His2 zinc finger motif
Istituto di Biostrutture e Bioimmagini, Via Mezzocannone 6, 80134 Napoli, Italy, 1 Dipartimento di Scienze Ambientali, Seconda Università degli Studi di Napoli, Via Vivaldi 43, 81100 Caserta, Italy and 2 Department of Biochemistry and Molecular Biology and Chemistry, University of Georgia, Athens, GA 30602, USA
*To whom correspondence should be addressed. Tel: +39 0823 274598; Fax: +39 0823 274605; Email: paolov.pedone{at}unina2.it
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors
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 determined 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 association 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.
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