8RZA

Ribonuclease W

Summary for 8RZA

• Entry DOI: 10.2210/pdb8rza/pdb
• Descriptor: Probable ribonuclease FAU-1, RNA (5'-R(P*UP*UP*U)-3'), RNA (5'-R(*UP*AP*U)-3'), ... (7 entities in total)
• Functional Keywords: rnase w, ribonuclease w, fau-1, archaea, ribosome biogenesis, hydrolase
• Biological source: Pyrococcus furiosus; More
• Total number of polymer chains: 3
• Total formula weight: 56149.81

Authors

Vayssieres, M.,Blaud, M.,Leulliot, N. (deposition date: 2024-02-12, release date: 2024-11-06, Last modification date: 2024-12-04)

Primary citation

Vayssieres, M.,Juttner, M.,Haas, K.,Ancelin, A.,Marchfelder, A.,Leulliot, N.,Ferreira-Cerca, S.,Blaud, M.
RNase W, a conserved ribonuclease family with a novel active site.
Nucleic Acids Res., 52:13386-13401, 2024

PubMed Abstract: Ribosome biogenesis is a complex process requiring multiple precursor ribosomal RNA (rRNA) cleavage steps. In archaea, the full set of ribonucleases (RNases) involved in rRNA processing remains to be discovered. A previous study suggested that FAU-1, a conserved protein containing an RNase G/E-like protein domain fused to a domain of unknown function (DUF402), acts as an RNase in archaea. However, the molecular basis of this activity remained so far elusive. Here, we report two X-ray crystallographic structures of RNase G/E-like-DUF402 hybrid proteins from Pyrococcus furiosus and Sulfolobus acidocaldarius, at 2.1 and 2.0 Å, respectively. The structures highlight a structural homology with the 5' RNA recognition domain of Escherichia coli RNase E but no homology with other known catalytic nuclease domains. Surprisingly, we demonstrate that the C-terminal domain of this hybrid protein, annotated as a putative diphosphatase domain, harbors the RNase activity. Our functional analysis also supports a model by which the RNase G/E-like domain acts as a regulatory subunit of the RNase activity. Finally, in vivo experiments in Haloferax volcanii suggest that this RNase participates in the maturation of pre-16S rRNA. Together, our study defines a new RNase family, which we termed the RNase W family, as the first archaea-specific contributor to archaeal ribosome biogenesis.

PubMed: 39445822
DOI: 10.1093/nar/gkae907

Experimental method

X-RAY DIFFRACTION (2.1 Å)