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Title:
Eri1 degrades the stem-loop of oligouridylated histone mRNAs to induce replication-dependent decay | Nature Structural & Molecular Biology
Description:
The exoribonuclease Eri1 binds the stem-loop of histone mRNAs, but the functional significance of this interaction has been unclear. New studies now indicate that 3A oligouridylation of histone mRNAs enables the Lsm1–7 complex to bind the oligo(U) tail and to interact with Eri1, whose catalytic activity degrades the double-stranded stem-loop structure. The exoRNase Eri1 inhibits RNA interference and trims the 5.8S rRNA 3′ end. It also binds to the stem-loop of histone mRNAs, but the functional importance of this interaction remains elusive. Histone mRNAs are normally degraded at the end of S phase or after pharmacological inhibition of replication. Both processes are impaired in Eri1-deficient mouse cells, which instead accumulate oligouridylated histone mRNAs. Eri1 trims the mature histone mRNAs by two unpaired nucleotides at the 3′ end but stalls close to the double-stranded stem. Upon oligouridylation of the histone mRNA, the Lsm1–7 heteroheptamer recognizes the oligo(U) tail and interacts with Eri1, whose catalytic activity is then able to degrade the stem-loop in a stepwise manner. These data demonstrate how degradation of histone mRNAs is initiated when 3′ oligouridylation creates a cis element that enables Eri1 to process the double-stranded stem-loop structure.
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Topics {✒️}
nature portfolio permissions reprints privacy policy mouse lymphocyte development german research foundation advertising cancer research social media nature 427 nature 404 nature double-stranded stem-loop structure eri1-deficient mouse cells induce replication-dependent decay conserved c-terminal sequence heterochromatin-dependent gene silencing complex protein-dna dynamics flag-ha-heri1 construct author correspondence replication-linked histone genes stem-loop binding protein springerlink instant access u-rich rna vigo heissmeyer mammalian histone pre-mrna zcchc11-dependent uridylation targets argonaute proteins permissions farm animal biology double-stranded stem gene silencing factor personal data general translational repression roquin promotes recognition stem-loop structure privacy conserved dual role oligouridylated histone mrnas dna replication type elisabeth kremmer lsm1–7 heteroheptamer recognizes probable regulatory roles present address competing financial interests mature histone mrnas cytoplasmic rna data protection data demonstrate histone mrna stability mouse eri1 interacts
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headline:Eri1 degrades the stem-loop of oligouridylated histone mRNAs to induce replication-dependent decay
description:The exoribonuclease Eri1 binds the stem-loop of histone mRNAs, but the functional significance of this interaction has been unclear. New studies now indicate that 3A oligouridylation of histone mRNAs enables the Lsm1â7 complex to bind the oligo(U) tail and to interact with Eri1, whose catalytic activity degrades the double-stranded stem-loop structure. The exoRNase Eri1 inhibits RNA interference and trims the 5.8S rRNA 3â² end. It also binds to the stem-loop of histone mRNAs, but the functional importance of this interaction remains elusive. Histone mRNAs are normally degraded at the end of S phase or after pharmacological inhibition of replication. Both processes are impaired in Eri1-deficient mouse cells, which instead accumulate oligouridylated histone mRNAs. Eri1 trims the mature histone mRNAs by two unpaired nucleotides at the 3â² end but stalls close to the double-stranded stem. Upon oligouridylation of the histone mRNA, the Lsm1â7 heteroheptamer recognizes the oligo(U) tail and interacts with Eri1, whose catalytic activity is then able to degrade the stem-loop in a stepwise manner. These data demonstrate how degradation of histone mRNAs is initiated when 3â² oligouridylation creates a cis element that enables Eri1 to process the double-stranded stem-loop structure.
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RNA decay
Structural biology
Life Sciences
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Protein Structure
Membrane Biology
Biological Microscopy
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headline:Eri1 degrades the stem-loop of oligouridylated histone mRNAs to induce replication-dependent decay
description:The exoribonuclease Eri1 binds the stem-loop of histone mRNAs, but the functional significance of this interaction has been unclear. New studies now indicate that 3A oligouridylation of histone mRNAs enables the Lsm1â7 complex to bind the oligo(U) tail and to interact with Eri1, whose catalytic activity degrades the double-stranded stem-loop structure. The exoRNase Eri1 inhibits RNA interference and trims the 5.8S rRNA 3â² end. It also binds to the stem-loop of histone mRNAs, but the functional importance of this interaction remains elusive. Histone mRNAs are normally degraded at the end of S phase or after pharmacological inhibition of replication. Both processes are impaired in Eri1-deficient mouse cells, which instead accumulate oligouridylated histone mRNAs. Eri1 trims the mature histone mRNAs by two unpaired nucleotides at the 3â² end but stalls close to the double-stranded stem. Upon oligouridylation of the histone mRNA, the Lsm1â7 heteroheptamer recognizes the oligo(U) tail and interacts with Eri1, whose catalytic activity is then able to degrade the stem-loop in a stepwise manner. These data demonstrate how degradation of histone mRNAs is initiated when 3â² oligouridylation creates a cis element that enables Eri1 to process the double-stranded stem-loop structure.
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Structural biology
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Protein Structure
Membrane Biology
Biological Microscopy
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