Academic Journal

Chemoproteomic discovery of a human RNA ligase

التفاصيل البيبلوغرافية
العنوان: Chemoproteomic discovery of a human RNA ligase
المؤلفون: Yuan, Yizhi, Stumpf, Florian M., Schmidt, Olivia, Saumer, Philip, Huber, Luisa B., Frese, Matthias, Höllmüller, Eva, Scheffner, Martin, Stengel, Florian, Diederichs, Kay, Marx, Andreas
المصدر: Nature Communications. Nature Publishing Group. 2023, 14, 842. eISSN 2041-1723. Available under: doi:10.1038/s41467-023-36451-x
سنة النشر: 2023
المجموعة: University of Konstanz: Konstanz Online Publication Server (KOPS)
مصطلحات موضوعية: ddc:570
الوصف: RNA ligases are present across all forms of life. While enzymatic RNA ligation between 5′-PO4 and 3′-OH termini is prevalent in viruses, fungi, and plants, such RNA ligases are yet to be identified in vertebrates. Here, using a nucleotide-based chemical probe targeting human AMPylated proteome, we have enriched and identified the hitherto uncharacterised human protein chromosome 12 open reading frame 29 (C12orf29) as a human enzyme promoting RNA ligation between 5′-PO4 and 3′-OH termini. C12orf29 catalyses ATP-dependent RNA ligation via a three-step mechanism, involving tandem auto- and RNA AMPylation. Knock-out of C12ORF29 gene impedes the cellular resilience to oxidative stress featuring concurrent RNA degradation, which suggests a role of C12orf29 in maintaining RNA integrity. These data provide the groundwork for establishing a human RNA repair pathway. ; published
نوع الوثيقة: article in journal/newspaper
وصف الملف: application/pdf
اللغة: English
ردمك: 978-1-83706-174-7
1-83706-174-2
Relation: http://nbn-resolving.de/urn:nbn:de:bsz:352-2-9hn573vvaei94; http://dx.doi.org/10.1038/s41467-023-36451-x
DOI: 10.1038/s41467-023-36451-x
الاتاحة: http://nbn-resolving.de/urn:nbn:de:bsz:352-2-9hn573vvaei94
https://doi.org/10.1038/s41467-023-36451-x
Rights: https://rightsstatements.org/page/InC/1.0/
رقم الانضمام: edsbas.586CAAD
قاعدة البيانات: BASE
الوصف
ردمك:9781837061747
1837061742
DOI:10.1038/s41467-023-36451-x