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We began analyzing https://www.nature.com/articles/nsmb1100, but it redirected us to https://www.nature.com/articles/nsmb1100. The analysis below is for the second page.

Title[redir]:
PUF proteins bind Pop2p to regulate messenger RNAs | Nature Structural & Molecular Biology
Description:
PUF proteins, a family of RNA-binding proteins, interact with the 3′ untranslated regions (UTRs) of specific mRNAs to control their translation and stability. PUF protein action is commonly correlated with removal of the poly(A) tail of target mRNAs. Here, we focus on how PUF proteins enhance deadenylation and mRNA decay. We show that a yeast PUF protein physically binds Pop2p, which is a component of the Ccr4p–Pop2p–Not deadenylase complex, and that Pop2p is required for PUF repression activity. By binding Pop2p, the PUF protein simultaneously recruits the Ccr4p deadenylase and two other enzymes involved in mRNA regulation, Dcp1p and Dhh1p. We reconstitute regulated deadenylation in vitro and demonstrate that the PUF-Pop2p interaction is conserved in yeast, worms and humans. We suggest that the PUF-Pop2p interaction underlies regulated deadenylation, mRNA decay and repression by PUF proteins.

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  • Education
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🏙️ Massive Traffic: 50M - 100M visitors per month


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Keywords {🔍}

pubmed, article, google, scholar, cas, nature, central, mrna, puf, yeast, proteins, access, deadenylase, protein, rna, biol, molecular, wickens, cell, content, biology, deadenylation, complex, translational, cookies, control, polya, regulation, mol, parker, drosophila, gene, caf, privacy, popp, family, decay, binding, open, pumilio, embo, regulates, function, data, structural, goldstrohm, hook, translation, nat, development,

Topics {✒️}

nature portfolio permissions reprints research grant privacy policy advertising nature 417 nature 425 nature social media author information authors author correspondence personal data molecular biology seay & marvin wickens translation factor eif-4e springerlink instant access data protection puf-pop2p interaction permissions puf protein action reconstitute regulated deadenylation controls postsynaptic accumulation elegans puf protein larval development puf family portrait post-transcriptional regulation rna-binding proteins yeast pop2 protein privacy regulate messenger rnas promoting posterior deadenylation competing financial interests messenger rna occur explore content subscription content drosophila body pattern saccharomyces cerevisiae permit drosophila oogenesis marvin wickens regulates cyclin poly development 124 development 132 european economic area institutional subscriptions read x-ray structure nucleic acid res nucleic acids res oligo-astheno-teratozoospermia mice lacking cnot7 dead box helicase

Schema {🗺️}

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         description:PUF proteins, a family of RNA-binding proteins, interact with the 3′ untranslated regions (UTRs) of specific mRNAs to control their translation and stability. PUF protein action is commonly correlated with removal of the poly(A) tail of target mRNAs. Here, we focus on how PUF proteins enhance deadenylation and mRNA decay. We show that a yeast PUF protein physically binds Pop2p, which is a component of the Ccr4p–Pop2p–Not deadenylase complex, and that Pop2p is required for PUF repression activity. By binding Pop2p, the PUF protein simultaneously recruits the Ccr4p deadenylase and two other enzymes involved in mRNA regulation, Dcp1p and Dhh1p. We reconstitute regulated deadenylation in vitro and demonstrate that the PUF-Pop2p interaction is conserved in yeast, worms and humans. We suggest that the PUF-Pop2p interaction underlies regulated deadenylation, mRNA decay and repression by PUF proteins.
         datePublished:2006-05-21T00:00:00Z
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      headline:PUF proteins bind Pop2p to regulate messenger RNAs
      description:PUF proteins, a family of RNA-binding proteins, interact with the 3′ untranslated regions (UTRs) of specific mRNAs to control their translation and stability. PUF protein action is commonly correlated with removal of the poly(A) tail of target mRNAs. Here, we focus on how PUF proteins enhance deadenylation and mRNA decay. We show that a yeast PUF protein physically binds Pop2p, which is a component of the Ccr4p–Pop2p–Not deadenylase complex, and that Pop2p is required for PUF repression activity. By binding Pop2p, the PUF protein simultaneously recruits the Ccr4p deadenylase and two other enzymes involved in mRNA regulation, Dcp1p and Dhh1p. We reconstitute regulated deadenylation in vitro and demonstrate that the PUF-Pop2p interaction is conserved in yeast, worms and humans. We suggest that the PUF-Pop2p interaction underlies regulated deadenylation, mRNA decay and repression by PUF proteins.
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