{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Machado de Amorim A"],"funding":["Deutsche Forschungsgemeinschaft","Deutsche Forschungsgemeinschaft (German Research Foundation)"],"pagination":["155"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12775136"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(1)"],"pubmed_abstract":["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"],"journal":["Nature communications"],"pubmed_title":["Mechanistic insights into recruitment and regulation of the RNA helicase UPF1 in replication-dependent histone mRNA decay."],"pmcid":["PMC12775136"],"funding_grant_id":["CH1245/6-1","CH1245/3-2","CH1245/5-1"],"pubmed_authors":["Xue G","Dittmers T","Lewandowski S","Urlaub H","Perez-Borrajero C","Hilal T","Nandana V","Machado de Amorim A","Marzluff WF","Mateva N","He W","Krage C","Loll B","Hennig J","Chakrabarti S","Bethmann J"],"additional_accession":[]},"is_claimable":false,"name":"Mechanistic insights into recruitment and regulation of the RNA helicase UPF1 in replication-dependent histone mRNA decay.","description":"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","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-06T11:52:11.585Z","creation":"2026-05-30T03:09:31.106Z"},"accession":"S-EPMC12775136","cross_references":{"pubmed":["41484129"],"doi":["10.1038/s41467-025-67991-z"]}}