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==Crystal structure of the Pumilio-Nos-CyclinB RNA complex==
==Crystal structure of the Pumilio-Nos-CyclinB RNA complex==
<StructureSection load='5kl8' size='340' side='right' caption='[[5kl8]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
<StructureSection load='5kl8' size='340' side='right'caption='[[5kl8]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5kl8]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KL8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5kl8]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KL8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kl1|5kl1]], [[5kla|5kla]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5kl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kl8 OCA], [http://pdbe.org/5kl8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kl8 RCSB], [http://www.ebi.ac.uk/pdbsum/5kl8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kl8 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5kl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kl8 OCA], [https://pdbe.org/5kl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kl8 RCSB], [https://www.ebi.ac.uk/pdbsum/5kl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kl8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PUM_DROME 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.<ref>PMID:1459455</ref> <ref>PMID:1576962</ref> <ref>PMID:9660969</ref>  [[http://www.uniprot.org/uniprot/NANOS_DROME NANOS_DROME]] Maternal RNA-binding protein that is required for germ cells proliferation and self-renewal. Acts by forming a complex with pum and brat that regulates translation and mRNA stability. The complex binds to the Nanos Response Element (NRE), a 16 bp sequence in the hb mRNA 3'-UTR and prevents its translation. Controls posterior development. Rescuing factor for the abdominal defect of posterior group mutants. The other posterior group genes are not required for nanos function but rather play a role in localization or distribution of nanos protein.
[https://www.uniprot.org/uniprot/PUM_DROME 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.<ref>PMID:1459455</ref> <ref>PMID:1576962</ref> <ref>PMID:9660969</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Collaboration among the multitude of RNA-binding proteins (RBPs) is ubiquitous, yet our understanding of these key regulatory complexes has been limited to single RBPs. We investigated combinatorial translational regulation by Drosophila Pumilio (Pum) and Nanos (Nos), which control development, fertility, and neuronal functions. Our results show how the specificity of one RBP (Pum) is modulated by cooperative RNA recognition with a second RBP (Nos) to synergistically repress mRNAs. Crystal structures of Nos-Pum-RNA complexes reveal that Nos embraces Pum and RNA, contributes sequence-specific contacts, and increases Pum RNA-binding affinity. Nos shifts the recognition sequence and promotes repression complex formation on mRNAs that are not stably bound by Pum alone, explaining the preponderance of sub-optimal Pum sites regulated in vivo. Our results illuminate the molecular mechanism of a regulatory switch controlling crucial gene expression programs, and provide a framework for understanding how the partnering of RBPs evokes changes in binding specificity that underlie regulatory network dynamics.
 
Drosophila Nanos acts as a molecular clamp that modulates the RNA-binding and repression activities of Pumilio.,Weidmann CA, Qiu C, Arvola RM, Lou TF, Killingsworth J, Campbell ZT, Tanaka Hall TM, Goldstrohm AC Elife. 2016 Aug 2;5. pii: e17096. doi: 10.7554/eLife.17096. PMID:27482653<ref>PMID:27482653</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kl8" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Hall, T M.T]]
[[Category: Drosophila melanogaster]]
[[Category: Qiu, C]]
[[Category: Large Structures]]
[[Category: Rna-binding protein-rna complex]]
[[Category: Hall TMT]]
[[Category: Rna-binding protein]]
[[Category: Qiu C]]

Latest revision as of 15:40, 6 March 2024

Crystal structure of the Pumilio-Nos-CyclinB RNA complexCrystal structure of the Pumilio-Nos-CyclinB RNA complex

Structural highlights

5kl8 is a 3 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

References

  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

5kl8, resolution 4.00Å

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