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Membrane Recognition and Dynamics of the RNA Degradosome


Recent discoveries that two ribonucleases with major roles in mRNA degradation, RNase E of Escherichia coli and RNase Y of Bacillus subtilis, are localized to the inner cytoplasmic membrane suggest that spatial separation of transcription and mRNA degradation are general features of the bacterial cell. Here we show that RNase E rapidly diffuses over the entire inner membrane forming short-lived foci. Results of molecular dynamics simulations lead us to suggest that RNase E interacts with the lipid membrane by a novel mechanism permitting a high degree of translational freedom. We show that RNA substrate is necessary for the formation of RNase E foci and that formation of foci correlates with constraints on the diffusion of RNase E. We therefore propose that foci are degradation bodies in which several RNase E molecules engage an RNA substrate. The sequestration of the mRNA degradation machinery to the inner cytoplasmic membrane has important consequences for mRNA turnover. This organization likely favors formation of polyribosomes on nascent transcripts before they are exposed to the degradation machinery. Rapid diffusion of RNase E on the inner cytoplasmic membrane could be part of a scanning mechanism that facilitates recognition of cytoplasmic polyribosomes and cooperative degradation of mRNA.


Vyšlo v časopise: Membrane Recognition and Dynamics of the RNA Degradosome. PLoS Genet 11(2): e32767. doi:10.1371/journal.pgen.1004961
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1004961

Souhrn

Recent discoveries that two ribonucleases with major roles in mRNA degradation, RNase E of Escherichia coli and RNase Y of Bacillus subtilis, are localized to the inner cytoplasmic membrane suggest that spatial separation of transcription and mRNA degradation are general features of the bacterial cell. Here we show that RNase E rapidly diffuses over the entire inner membrane forming short-lived foci. Results of molecular dynamics simulations lead us to suggest that RNase E interacts with the lipid membrane by a novel mechanism permitting a high degree of translational freedom. We show that RNA substrate is necessary for the formation of RNase E foci and that formation of foci correlates with constraints on the diffusion of RNase E. We therefore propose that foci are degradation bodies in which several RNase E molecules engage an RNA substrate. The sequestration of the mRNA degradation machinery to the inner cytoplasmic membrane has important consequences for mRNA turnover. This organization likely favors formation of polyribosomes on nascent transcripts before they are exposed to the degradation machinery. Rapid diffusion of RNase E on the inner cytoplasmic membrane could be part of a scanning mechanism that facilitates recognition of cytoplasmic polyribosomes and cooperative degradation of mRNA.


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