Details
| Originalsprache | Englisch |
|---|---|
| Aufsatznummer | 17561 |
| Fachzeitschrift | Scientific reports |
| Jahrgang | 11 |
| Frühes Online-Datum | 2 Sept. 2021 |
| Publikationsstatus | Veröffentlicht - Dez. 2021 |
Abstract
Box C/D ribonucleoprotein complexes are RNA-guided methyltransferases that methylate the ribose 2’-OH of RNA. The central ‘guide RNA’ has box C and D motifs at its ends, which are crucial for activity. Archaeal guide RNAs have a second box C’/D’ motif pair that is also essential for function. This second motif is poorly conserved in eukaryotes and its function is uncertain. Conflicting literature data report that eukaryotic box C’/D’ motifs do or do not bind proteins specialized to recognize box C/D-motifs and are or are not important for function. Despite this uncertainty, the architecture of eukaryotic 2’-O-methylation enzymes is thought to be similar to that of their archaeal counterpart. Here, we use biochemistry, X-ray crystallography and mutant analysis to demonstrate the absence of functional box C’/D’ motifs in more than 80% of yeast guide RNAs. We conclude that eukaryotic Box C/D RNPs have two non-symmetric protein assembly sites and that their three-dimensional architecture differs from that of archaeal 2’-O-methylation enzymes.
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in: Scientific reports, Jahrgang 11, 17561, 12.2021.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Eukaryotic Box C/D methylation machinery has two non-symmetric protein assembly sites
AU - Höfler, Simone
AU - Lukat, Peer
AU - Blankenfeldt, Wulf
AU - Carlomagno, Teresa
N1 - Funding Information: Open Access funding enabled and organized by Projekt DEAL. This work was funded by the Deutsche Forschun-gsgemeinschaft through a project grant to T.C. in the frame of the priority program “Chemical Biology of Natural Nucleic Acids Modifications” (CA 294/11–1).
PY - 2021/12
Y1 - 2021/12
N2 - Box C/D ribonucleoprotein complexes are RNA-guided methyltransferases that methylate the ribose 2’-OH of RNA. The central ‘guide RNA’ has box C and D motifs at its ends, which are crucial for activity. Archaeal guide RNAs have a second box C’/D’ motif pair that is also essential for function. This second motif is poorly conserved in eukaryotes and its function is uncertain. Conflicting literature data report that eukaryotic box C’/D’ motifs do or do not bind proteins specialized to recognize box C/D-motifs and are or are not important for function. Despite this uncertainty, the architecture of eukaryotic 2’-O-methylation enzymes is thought to be similar to that of their archaeal counterpart. Here, we use biochemistry, X-ray crystallography and mutant analysis to demonstrate the absence of functional box C’/D’ motifs in more than 80% of yeast guide RNAs. We conclude that eukaryotic Box C/D RNPs have two non-symmetric protein assembly sites and that their three-dimensional architecture differs from that of archaeal 2’-O-methylation enzymes.
AB - Box C/D ribonucleoprotein complexes are RNA-guided methyltransferases that methylate the ribose 2’-OH of RNA. The central ‘guide RNA’ has box C and D motifs at its ends, which are crucial for activity. Archaeal guide RNAs have a second box C’/D’ motif pair that is also essential for function. This second motif is poorly conserved in eukaryotes and its function is uncertain. Conflicting literature data report that eukaryotic box C’/D’ motifs do or do not bind proteins specialized to recognize box C/D-motifs and are or are not important for function. Despite this uncertainty, the architecture of eukaryotic 2’-O-methylation enzymes is thought to be similar to that of their archaeal counterpart. Here, we use biochemistry, X-ray crystallography and mutant analysis to demonstrate the absence of functional box C’/D’ motifs in more than 80% of yeast guide RNAs. We conclude that eukaryotic Box C/D RNPs have two non-symmetric protein assembly sites and that their three-dimensional architecture differs from that of archaeal 2’-O-methylation enzymes.
UR - http://www.scopus.com/inward/record.url?scp=85114630818&partnerID=8YFLogxK
U2 - 10.1038/s41598-021-97030-y
DO - 10.1038/s41598-021-97030-y
M3 - Article
C2 - 34475498
AN - SCOPUS:85114630818
VL - 11
JO - Scientific reports
JF - Scientific reports
SN - 2045-2322
M1 - 17561
ER -