5m0j

Crystal structure of the cytoplasmic complex with She2p, She3p, and the ASH1 mRNA E3-localization element

spinqualitylabelsall models 5m0j, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5m0j is a 10 chain structure with sequence from Saccharomyces cerevisiae and Saccharomyces cerevisiae RM11-1a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SHE3_YEAST 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. Required for the delivery of cortical endoplasmic reticulum into the emerging bud. SHE2_YEAST 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. Recruites also LOC1 and PUF6 to ASH1 mRNA, which are required for translational repression of this mRNA. 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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