SNAP output for PDB entry 8rza [SNAP web server]

PDB-id

8rza; SNAP-derived features in text and JSON formats; DNAproDB

Class

hydrolase

Method

X-ray (2.1 Å)

Summary

Ribonuclease w

Reference

Vayssieres M, Juttner M, Haas K, Ancelin A, Marchfelder A, Leulliot N, Ferreira-Cerca S, Blaud M (2024): "RNase W, a conserved ribonuclease family with a novel active site." Nucleic Acids Res. doi: 10.1093/nar/gkae907.

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.