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J Biol Chem, Vol. 273, Issue 43, 28504-28509, October 23, 1998
From the Institute of Genetics, Free University Berlin, Arnimallee
7, D-14195 Berlin, Germany
Pipsqueak (Psq) belongs to a family of proteins
defined by a phylogenetically old protein-protein interaction motif.
Like the GAGA factor and other members of this family, Psq is an
important developmental regulator in Drosophila, having
pleiotropic functions during oogenesis, embryonic pattern formation,
and adult development. The GAGA factor controls the transcriptional
activation of homeotic genes and other genes by binding to control
elements containing the GAGAG consensus motif. Binding is associated
with formation of an open chromatin structure that makes the control
regions accessible to transcriptional activators. We show here that Psq contains a novel DNA-binding domain, which binds, like the GAGA factor
zinc finger DNA-binding domain, to target sites containing the GAGAG
consensus motif. Binding is suppressed, as in the GAGA factor and other
proteins of the family, by the associated protein-protein interaction
motif. The DNA-binding domain, which we call the Psq domain, is
identical with a previously identified region consisting of four tandem
repeats of a conserved 50-amino acid sequence, the Psq motif. The Psq
domain seems to be structurally related to known DNA-binding domains,
both in its repetitive character and in the putative three-
The Pipsqueak Protein of Drosophila melanogaster
Binds to GAGA Sequences through a Novel DNA-binding Domain
-helix
structure of the Psq motif, but it lacks the conserved sequence
signatures of the classical eukaryotic DNA-binding motifs. Psq may thus
represent the prototype of a new family of DNA-binding proteins.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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