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5m0j
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/SHE2_YEAS1 SHE2_YEAS1]] RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruits the MYO4-SHE3 complex to the ASH1 mRNA. Recruits also LOC1 and PUF6 to ASH1 mRNA, which are required for translational repression of this mRNA (By similarity). | [[http://www.uniprot.org/uniprot/SHE2_YEAS1 SHE2_YEAS1]] RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruits the MYO4-SHE3 complex to the ASH1 mRNA. Recruits also LOC1 and PUF6 to ASH1 mRNA, which are required for translational repression of this mRNA (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | mRNA localization is an essential mechanism of gene regulation and is required for processes such as stem-cell division, embryogenesis and neuronal plasticity. It is not known which features in the cis-acting mRNA localization elements (LEs) are specifically recognized by motor-containing transport complexes. To the best of our knowledge, no high-resolution structure is available for any LE in complex with its cognate protein complex. Using X-ray crystallography and complementary techniques, we carried out a detailed assessment of an LE of the ASH1 mRNA from yeast, its complex with its shuttling RNA-binding protein She2p, and its highly specific, cytoplasmic complex with She3p. Although the RNA alone formed a flexible stem loop, She2p binding induced marked conformational changes. However, only joining by the unstructured She3p resulted in specific RNA recognition. The notable RNA rearrangements and joint action of a globular and an unfolded RNA-binding protein offer unprecedented insights into the step-wise maturation of an mRNA-transport complex. | ||
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| + | Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex.,Edelmann FT, Schlundt A, Heym RG, Jenner A, Niedner-Boblenz A, Syed MI, Paillart JC, Stehle R, Janowski R, Sattler M, Jansen RP, Niessing D Nat Struct Mol Biol. 2017 Jan 16. doi: 10.1038/nsmb.3351. PMID:28092367<ref>PMID:28092367</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5m0j" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 16:18, 25 January 2017
Crystal structure of the cytoplasmic complex with She2p, She3p, and the ASH1 mRNA E3-localization element
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