3h3d

Drosophila Pumilio RNA binding domain (Puf domain)Drosophila Pumilio RNA binding domain (Puf domain)

Structural highlights

3h3d is a 2 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	pumilio (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[PUM_DROME] Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding to the Nanos Response Element (NRE), a 16 bp sequence in the hb mRNA 3'-UTR and prevents its translation. Required for abdominal development and to support proliferation and self-renewal of germ cells. Pum is the only gene required for nos activity that is not also required for posterior localization of germline determinants. Pum is required during embryogenesis when nos activity apparently moves anteriorly from the posterior pole.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Translation regulation plays an essential role in the differentiation and development of animal cells. One well-studied case is the control of hunchback mRNA during early Drosophila embryogenesis by the trans-acting factors Pumilio, Nanos, and Brain Tumor. We report here a crystal structure of the critical region of Pumilio, the Puf domain, that organizes a multivalent repression complex on the 3' untranslated region of hunchback mRNA. The structure reveals an extended, rainbow shaped molecule, with tandem helical repeats that bear unexpected resemblance to the armadillo repeats in beta-catenin and the HEAT repeats in protein phosphatase 2A. Based on the structure and genetic experiments, we identify putative interaction surfaces for hunchback mRNA and the cofactors Nanos and Brain Tumor. This analysis suggests that similar features in helical repeat proteins are used to bind extended peptides and RNA.

Structure of Pumilio reveals similarity between RNA and peptide binding motifs.,Edwards TA, Pyle SE, Wharton RP, Aggarwal AK Cell. 2001 Apr 20;105(2):281-9. PMID:11336677^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Barker DD, Wang C, Moore J, Dickinson LK, Lehmann R. Pumilio is essential for function but not for distribution of the Drosophila abdominal determinant Nanos. Genes Dev. 1992 Dec;6(12A):2312-26. PMID:1459455
↑ Macdonald PM. The Drosophila pumilio gene: an unusually long transcription unit and an unusual protein. Development. 1992 Jan;114(1):221-32. PMID:1576962
↑ Wharton RP, Sonoda J, Lee T, Patterson M, Murata Y. The Pumilio RNA-binding domain is also a translational regulator. Mol Cell. 1998 May;1(6):863-72. PMID:9660969
↑ Edwards TA, Pyle SE, Wharton RP, Aggarwal AK. Structure of Pumilio reveals similarity between RNA and peptide binding motifs. Cell. 2001 Apr 20;105(2):281-9. PMID:11336677

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OCA

[1] Barker DD, Wang C, Moore J, Dickinson LK, Lehmann R. Pumilio is essential for function but not for distribution of the Drosophila abdominal determinant Nanos. Genes Dev. 1992 Dec;6(12A):2312-26. PMID:1459455

[2] Macdonald PM. The Drosophila pumilio gene: an unusually long transcription unit and an unusual protein. Development. 1992 Jan;114(1):221-32. PMID:1576962

[3] Wharton RP, Sonoda J, Lee T, Patterson M, Murata Y. The Pumilio RNA-binding domain is also a translational regulator. Mol Cell. 1998 May;1(6):863-72. PMID:9660969

[4] Edwards TA, Pyle SE, Wharton RP, Aggarwal AK. Structure of Pumilio reveals similarity between RNA and peptide binding motifs. Cell. 2001 Apr 20;105(2):281-9. PMID:11336677

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