Histone mRNA is subject to 3′ uridylation and re‐adenylation in Aspergillus nidulans

dc.contributor.authorMossanen-Parsi, Amir
dc.contributor.authorParisi, Daniele
dc.contributor.authorBrowne-Marke, Natasha
dc.contributor.authorBharudin, Izwan
dc.contributor.authorConnell, Sean R.
dc.contributor.authorMayans, Olga
dc.contributor.authorFucini, Paola
dc.contributor.authorMorozov, Igor Y.
dc.contributor.authorCaddick, Mark X.
dc.date.accessioned2020-11-25T12:43:25Z
dc.date.available2020-11-25T12:43:25Z
dc.date.issued2021-02
dc.description.abstractThe role of post‐transcriptional RNA modification is of growing interest. One example is the addition of non‐templated uridine residues to the 3′ end of transcripts. In mammalian systems, uridylation is integral to cell cycle control of histone mRNA levels. This regulatory mechanism is dependent on the nonsense‐mediated decay (NMD) component, Upf1, which promotes histone mRNA uridylation and degradation in response to the arrest of DNA synthesis. We have identified a similar system in Aspergillus nidulans, where Upf1 is required for the regulation of histone mRNA levels. However, other NMD components are also implicated, distinguishing it from the mammalian system. As in human cells, 3′ uridylation of histone mRNA is induced upon replication arrest. Disruption of this 3′ tagging has a significant but limited effect on histone transcript regulation, consistent with multiple mechanisms acting to regulate mRNA levels. Interestingly, 3′ end degraded transcripts are also subject to re‐adenylation. Both mRNA pyrimidine tagging and re‐adenylation are dependent on the same terminal‐nucleotidyltransferases, CutA, and CutB, and we show this is consistent with the in vitro activities of both enzymes. Based on these data we argue that mRNA 3′ tagging has diverse and distinct roles associated with transcript degradation, functionality and regulation.eng
dc.description.versionpublishedeng
dc.identifier.doi10.1111/mmi.14613eng
dc.identifier.pmid33047379eng
dc.identifier.ppn1755954379
dc.identifier.urihttps://kops.uni-konstanz.de/handle/123456789/51915
dc.language.isoengeng
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subject.ddc570eng
dc.titleHistone mRNA is subject to 3′ uridylation and re‐adenylation in Aspergillus nidulanseng
dc.typeJOURNAL_ARTICLEeng
dspace.entity.typePublication
kops.citation.bibtex
@article{MossanenParsi2021-02Histo-51915,
  year={2021},
  doi={10.1111/mmi.14613},
  title={Histone mRNA is subject to 3′ uridylation and re‐adenylation in Aspergillus nidulans},
  number={2},
  volume={115},
  issn={0950-382X},
  journal={Molecular Microbiology},
  pages={238--254},
  author={Mossanen-Parsi, Amir and Parisi, Daniele and Browne-Marke, Natasha and Bharudin, Izwan and Connell, Sean R. and Mayans, Olga and Fucini, Paola and Morozov, Igor Y. and Caddick, Mark X.}
}
kops.citation.iso690MOSSANEN-PARSI, Amir, Daniele PARISI, Natasha BROWNE-MARKE, Izwan BHARUDIN, Sean R. CONNELL, Olga MAYANS, Paola FUCINI, Igor Y. MOROZOV, Mark X. CADDICK, 2021. Histone mRNA is subject to 3′ uridylation and re‐adenylation in Aspergillus nidulans. In: Molecular Microbiology. Wiley. 2021, 115(2), pp. 238-254. ISSN 0950-382X. eISSN 1365-2958. Available under: doi: 10.1111/mmi.14613deu
kops.citation.iso690MOSSANEN-PARSI, Amir, Daniele PARISI, Natasha BROWNE-MARKE, Izwan BHARUDIN, Sean R. CONNELL, Olga MAYANS, Paola FUCINI, Igor Y. MOROZOV, Mark X. CADDICK, 2021. Histone mRNA is subject to 3′ uridylation and re‐adenylation in Aspergillus nidulans. In: Molecular Microbiology. Wiley. 2021, 115(2), pp. 238-254. ISSN 0950-382X. eISSN 1365-2958. Available under: doi: 10.1111/mmi.14613eng
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    <dcterms:abstract xml:lang="eng">The role of post‐transcriptional RNA modification is of growing interest. One example is the addition of non‐templated uridine residues to the 3′ end of transcripts. In mammalian systems, uridylation is integral to cell cycle control of histone mRNA levels. This regulatory mechanism is dependent on the nonsense‐mediated decay (NMD) component, Upf1, which promotes histone mRNA uridylation and degradation in response to the arrest of DNA synthesis. We have identified a similar system in Aspergillus nidulans, where Upf1 is required for the regulation of histone mRNA levels. However, other NMD components are also implicated, distinguishing it from the mammalian system. As in human cells, 3′ uridylation of histone mRNA is induced upon replication arrest. Disruption of this 3′ tagging has a significant but limited effect on histone transcript regulation, consistent with multiple mechanisms acting to regulate mRNA levels. Interestingly, 3′ end degraded transcripts are also subject to re‐adenylation. Both mRNA pyrimidine tagging and re‐adenylation are dependent on the same terminal‐nucleotidyltransferases, CutA, and CutB, and we show this is consistent with the in vitro activities of both enzymes. Based on these data we argue that mRNA 3′ tagging has diverse and distinct roles associated with transcript degradation, functionality and regulation.</dcterms:abstract>
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kops.sourcefieldMolecular Microbiology. Wiley. 2021, <b>115</b>(2), pp. 238-254. ISSN 0950-382X. eISSN 1365-2958. Available under: doi: 10.1111/mmi.14613deu
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