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Keywords {🔍}

lsm, complex, decapping, patc, article, lsmpatc, mrna, google, scholar, cas, figure, pat, decay, data, interaction, structure, proteins, rna, helix, cell, lane, yeast, binding, protein, nature, interactions, human, residues, biol, information, model, mrnas, mol, ring, chain, degradation, shown, parker, vivo, dcpdcp, cterminal, loop, lsmpat, crystal, domain, face, lsmδα, mutations, similar, activity,

Topics {✒️}

nature portfolio privacy policy model-building tools au-rich element-mediated decay advertising cell research website [α-32p] gtp-labeled capping c-terminal alpha-alpha superhelix multiple-wavelength anomalous diffraction social media nature 1988 nature 1996 nature 2000 nature 2009 nature 2011 nature author information authors 0 reprints accession code 4n0a semet-substituted lsm2-3-pat1c proteins creative commons attribution-noncommercial research nonsense-mediated mrna decay homo-oligomeric rna-binding ability middle domain c-fos mrna facilitated author correspondence α-α superhelix surrounding human ortholog ddx6/rck yeast spliceosomal penta-snrnp microrna-mediated mrna decay1 putative rna-binding surface ta6br12-soaked lsm2-3-pat1c crystal structure-guided mutagenesis revealed c-terminal region truncated uridylation-mediated mrna decapping11 virus host-cell interactions rna-binding preference similar similar rna-binding properties similar rna-binding preference n-terminal α helix c-terminal α helix pei-cellulose tlc plates cap-labeled rna relative microrna-mediated translational repression protein data bank promote p-body assembly pat1 c-terminal domain mirna-mediated gene silencing group b-factors refinement

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      description:The evolutionarily conserved Lsm1-7-Pat1 complex is the most critical activator of mRNA decapping in eukaryotic cells and plays many roles in normal decay, AU-rich element-mediated decay, and miRNA silencing, yet how Pat1 interacts with the Lsm1-7 complex is unknown. Here, we show that Lsm2 and Lsm3 bridge the interaction between the C-terminus of Pat1 (Pat1C) and the Lsm1-7 complex. The Lsm2-3-Pat1C complex and the Lsm1-7-Pat1C complex stimulate decapping in vitro to a similar extent and exhibit similar RNA-binding preference. The crystal structure of the Lsm2-3-Pat1C complex shows that Pat1C binds to Lsm2-3 to form an asymmetric complex with three Pat1C molecules surrounding a heptameric ring formed by Lsm2-3. Structure-based mutagenesis revealed the importance of Lsm2-3-Pat1C interactions in decapping activation in vivo. Based on the structure of Lsm2-3-Pat1C, a model of Lsm1-7-Pat1 complex is constructed and how RNA binds to this complex is discussed.
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