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Mechanistic insights into recruitment and regulation of the RNA helicase UPF1 in replication-dependent histone mRNA decay

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Τίτλος: Mechanistic insights into recruitment and regulation of the RNA helicase UPF1 in replication-dependent histone mRNA decay
Συγγραφείς: Machado de Amorim, Alexandrina, Xue, Guangpu, He, Wenxia, Dittmers, Theresa, Lewandowski, Sarah, Perez-Borrajero, Cecilia, Bethmann, Juliane, Mateva, Nevena, Krage, Clemens, Nandana, Vidhyadhar, Loll, Bernhard, Hilal, Tarek, Hennig, Janosch, Urlaub, Henning, Marzluff, William F., Chakrabarti, Sutapa
Πηγή: Nature Communications, 17(1)
Στοιχεία εκδότη: Springer Nature
Έτος έκδοσης: 2026
Συλλογή: Carolina Digital Repository (UNC - University of North Carolina)
Θεματικοί όροι: tail, binding, intricate network, insights, cryoEM structure, activity, ATP, RNA binding, exoribonuclease, absence, activity of Upf1, stage, histone, histone mRNA degradation, metazoans, SLBP, core, melting, events, S phase, RNA stem, absence of ATP, evidence, interaction, molecular mechanisms, mRNA degradation, Metazoan histone mRNAs, complex, assembly, cellular analysis
Περιγραφή: Metazoan histone mRNAs are a unique class of mRNAs that lack the poly(A) tail present in all other eukaryotic transcripts. Instead, they end in a conserved stem-loop (SL) structure, necessitating a decay mechanism that is distinct from deadenylation-initiated degradation. Here, combining structural and functional approaches, we elucidate molecular mechanisms of initiation of histone mRNA decay. At the end of S-phase, the RNA helicase UPF1, the exoribonuclease 3’hExo and stem-loop binding protein SLBP all contribute to histone mRNA degradation, although how they are mechanistically coupled remained unknown. The cryoEM structure of an UPF1:SL RNA complex, presented here, shows that binding of UPF1 partially melts the RNA stem in the absence of ATP, harnessing the free energy derived from RNA-binding to unwind RNA. This melting event primes the SL-RNA for decay by 3’hExo. Using biochemical and cellular analyses, we demonstrate that SLBP directly engages the UPF1 helicase core to attenuate its unwinding activity and prevent premature degradation. Activation of UPF1 at a later stage promotes SL-RNA decay. We provide direct evidence that UPF1, SLBP and 3’hExo form a degradosome-like assembly that functionally couples SL unwinding and degradation, highlighting a dynamic and intricate network of UPF1-centric interactions that orchestrates timely histone mRNA decay.
Τύπος εγγράφου: article in journal/newspaper
Γλώσσα: unknown
Relation: https://cdr.lib.unc.edu/downloads/v692tq64h?file=thumbnail; https://cdr.lib.unc.edu/downloads/v692tq64h
DOI: 10.17615/0y6g-9j58
Διαθεσιμότητα: https://doi.org/10.17615/0y6g-9j58
https://cdr.lib.unc.edu/downloads/v692tq64h?file=thumbnail
https://cdr.lib.unc.edu/downloads/v692tq64h
Rights: http://rightsstatements.org/vocab/InC/1.0/ ; http://creativecommons.org/licenses/by/4.0/
Αριθμός Καταχώρησης: edsbas.96059ACC
Βάση Δεδομένων: BASE
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  – Url: https://doi.org/10.17615/0y6g-9j58#
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  Data: Mechanistic insights into recruitment and regulation of the RNA helicase UPF1 in replication-dependent histone mRNA decay
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  Data: Nature Communications, 17(1)
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  Data: Springer Nature
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  Data: 2026
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  Data: Carolina Digital Repository (UNC - University of North Carolina)
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  Data: Metazoan histone mRNAs are a unique class of mRNAs that lack the poly(A) tail present in all other eukaryotic transcripts. Instead, they end in a conserved stem-loop (SL) structure, necessitating a decay mechanism that is distinct from deadenylation-initiated degradation. Here, combining structural and functional approaches, we elucidate molecular mechanisms of initiation of histone mRNA decay. At the end of S-phase, the RNA helicase UPF1, the exoribonuclease 3’hExo and stem-loop binding protein SLBP all contribute to histone mRNA degradation, although how they are mechanistically coupled remained unknown. The cryoEM structure of an UPF1:SL RNA complex, presented here, shows that binding of UPF1 partially melts the RNA stem in the absence of ATP, harnessing the free energy derived from RNA-binding to unwind RNA. This melting event primes the SL-RNA for decay by 3’hExo. Using biochemical and cellular analyses, we demonstrate that SLBP directly engages the UPF1 helicase core to attenuate its unwinding activity and prevent premature degradation. Activation of UPF1 at a later stage promotes SL-RNA decay. We provide direct evidence that UPF1, SLBP and 3’hExo form a degradosome-like assembly that functionally couples SL unwinding and degradation, highlighting a dynamic and intricate network of UPF1-centric interactions that orchestrates timely histone mRNA decay.
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  Data: 10.17615/0y6g-9j58
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        Value: 10.17615/0y6g-9j58
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      – SubjectFull: tail
        Type: general
      – SubjectFull: binding
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      – SubjectFull: intricate network
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      – TitleFull: Mechanistic insights into recruitment and regulation of the RNA helicase UPF1 in replication-dependent histone mRNA decay
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