 Pumilio (PUF repeats) Domain | |
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Structure:
 The structure shown is of the human pumilio (Puf) domain-containing protein, Pumilio1, in complex with RNA. The 8 pumilio repeats bind RNA using the concave surface of the protein. Structurally, these domains are α-helical repeat proteins that bear some resemblance to the Armadillo (ARM) repeat proteins, β-catenin and karyopherin α.
Structure Reference:
Wang, X. et al. (2002) Cell. 110(4): 501-512. PDB: 1M8W.
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Domain binding and function:
The PUF family of proteins are highly conserved among organisms from yeast to humans and plants. All Pumilio/Puf proteins contain a C-terminal domain that consist of eight repeated sequence subunits with N- and C-terminal flanking regions termed the Pumilio homology domain. Pumulio repeat proteins regulate various aspects of development by controlling mRNA stability and translation through its sequence-specific interaction with the 3’untranslated region of target mRNAs. The affinity and specificity of the interaction of this domain and RNA is determined by the reiterated use of the individual Pumilio subunits that make contact with the RNA base using three conserved amino acid residues that contact individual RNA bases.
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Examples of Proteins:
| PUF domain proteins |
| Drosophila Pumilio |
| Human Pumilio1, 2 |
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Referenced in part on Cell Signaling Technology Website, Reference Section on Protein Domains. We gratefully acknowledge the following contributors:
Piers Nash1, Dan Lin3, Kathleen Binns2, Clark Wells2, Rob Ingham2, Terry Kubiseski2, Bernard Liu1, Matt Smith2,3, Ivan Blasutig2,3, Maria Sierra1, Caesar Lim2,3, Michael Arc1, Jim Fawcett2 and Tony Pawson2,3.
1. Ben May Institute for Cancer Research, The University of Chicago, Chicago, Illinois, 60637, USA
2. Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, M5G 1X5, Canada
3. Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada
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