|PROSITE documentation PDOC50302|
Members of the Pumilio family of proteins (Puf) regulate translation and mRNA stability in a wide variety of eukaryotic organisms including mammals, flies, worms, slime mold, and yeast . Pumilio family members are characterized by the presence of eight tandem copies of an imperfectly repeated 36 amino acids sequence motif, the Pumilio repeat, surrounded by a short N- and C-terminal conserved region. The eight repeats and the N- and C-terminal regions form the Pumilio homology domain (PUM-HD). The PUM-HD domain is a sequence-specific RNA binding domain. Several Puf members have been shown to bind specific RNA sequences mainly found in the 3' UTR of mRNA and repress their translation . Frequently, Puf proteins function asymmetrically to create protein gradients, thus causing asymmetric cell division and regulating cell fate specification .
Crystal structure of Pumilio repeats has been solved (see <PDB:1IB2>) . The PUM repeat with the N- and C-terminal regions pack together to form a right-handed superhelix that approximates a half doughnut structurally similar to the Armadillo (ARM) repeat proteins (see <PDOC50176>), β-catenin and karyopherin α. The RNA binds the concave surface of the molecule, where each of the protein's eight repeats makes contacts with a different RNA base via three amino acid side chains at conserved positions .
Some of the proteins known to contain Pumilio repeats are listed below:
Two profiles were developed for this conserved region, the first one picks up pumilio repeat units while the second one detects the whole PUM-HD domain.Last update:
January 2004 / First entry.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Parisi M. Lin H.|
|Title||Translational repression: a duet of Nanos and Pumilio.|
|Source||Curr. Biol. 10:R81-R83(2000).|
|2||Authors||Spassov D.S. Jurecic R.|
|Title||The PUF family of RNA-binding proteins: does evolutionarily conserved structure equal conserved function?|
|Source||IUBMB Life 55:359-366(2003).|
|3||Authors||Barker D.D. Wang C. Moore J. Dickinson L.K. Lehmann R.|
|Title||Pumilio is essential for function but not for distribution of the Drosophila abdominal determinant Nanos.|
|Source||Genes Dev. 6:2312-2326(1992).|
|4||Authors||Wang X. Zamore P.D. Hall T.M.|
|Title||Crystal structure of a Pumilio homology domain.|
|Source||Mol. Cell 7:855-865(2001).|
|5||Authors||Wang X. McLachlan J. Zamore P.D. Hall T.M.|
|Title||Modular recognition of RNA by a human pumilio-homology domain.|