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Mol Cell. 2018 Sep 20;71(6):1027-1039.e14. doi: 10.1016/j.molcel.2018.08.003. Epub 2018 Sep 6.

α-Proteobacterial RNA Degradosomes Assemble Liquid-Liquid Phase-Separated RNP Bodies.

Author information

1
Department of Biological Sciences, Wayne State University, Detroit, MI, 48202, USA.
2
Department of Chemistry, University of Pittsburgh, Pittsburgh, PA, 15260, USA.
3
Department of Chemistry, University of Pittsburgh, Pittsburgh, PA, 15260, USA. Electronic address: wschild@pitt.edu.
4
Department of Biological Sciences, Wayne State University, Detroit, MI, 48202, USA. Electronic address: schrader@wayne.edu.

Abstract

Ribonucleoprotein (RNP) granules play an important role in organizing eukaryotic mRNA metabolism via liquid-liquid phase separation (LLPS) of mRNA decay factors into membrane-less organelles in the cytoplasm. Here we show that the bacterium Caulobacter crescentus Ribonuclease (RNase) E assembles RNP LLPS condensates that we term bacterial RNP-bodies (BR-bodies), similar to eukaryotic P-bodies and stress granules. RNase E requires RNA to assemble a BR-body, and disassembly requires RNA cleavage, suggesting BR-bodies provide localized sites of RNA degradation. The unstructured C-terminal domain of RNase E is both necessary and sufficient to assemble the core of the BR-body, is functionally conserved in related α-proteobacteria, and influences mRNA degradation. BR-bodies are rapidly induced under cellular stresses and provide enhanced cell growth under stress. To our knowledge, Caulobacter RNase E is the first bacterial protein identified that forms LLPS condensates, providing an effective strategy for subcellular organization in cells lacking membrane-bound compartments.

KEYWORDS:

P-bodies; RNA degradation; RNase E; bacteria; liquid-liquid phase separation; mRNA decay; stress granules

PMID:
30197298
PMCID:
PMC6151146
DOI:
10.1016/j.molcel.2018.08.003
[Indexed for MEDLINE]
Free PMC Article

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