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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 [1]. 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 [2]. Frequently, Puf proteins function asymmetrically to create protein gradients, thus causing asymmetric cell division and regulating cell fate specification [3].
Crystal structure of Pumilio repeats has been solved (see <PDB:1IB2>) [4]. 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 [5].
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.
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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). | |
PubMed ID | 10662662 |
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). | |
PubMed ID | 14584586 |
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). | |
PubMed ID | 1459455 |
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). | |
PubMed ID | 11336708 |
5 | Authors | Wang X. McLachlan J. Zamore P.D. Hall T.M. |
Title | Modular recognition of RNA by a human pumilio-homology domain. | |
Source | Cell 110:501-512(2002). | |
PubMed ID | 12202039 |