[PDF] RNase Y in Bacillus subtilis: a Natively Disordered Protein That Is the Functional Equivalent of RNase E from Escherichia coli | Semantic Scholar (2024)

The findings suggest that the interactions of the enzymes involved in RNA degradation in B. subtilis are rather transient, and the bulk of these enzymes is located in the cytoplasm.

A model, based on recent published data, of RNA degradation in B. subtilis mRNAs is presented, which shows that degradation is initiated by RNase Y‐dependent endonucleolytic cleavage, followed by processive exoribon nucleolysis of the generated fragments both in 3‐to‐5′ and in 5‐to-3′ directions.

The effect of citrate, c-di-GMP and c- di-AMP, as well as enolase and phosphofructokinase, on the RNA degradation activity of PNPase is studied, which confirms the interaction of the RNases J1 and J2 through the C-terminal domain, and shows that they oligomerize as dimers and tetramers.

An overview of the data on interactions between Firmicute RNA degradation factors is gathered, to highlight the similarities and differences between experimental data from different experiments and from different organisms.

The data confirm that this endoribonuclease plays a key role in initiating the decay of a large number of mRNAs as well as non coding RNAs and confirm already known RNase Y substrates.

It is found that the Y-complex is required for the majority of RNase Y-mediated mRNA maturation events and also affects riboswitch abundance in B. subtilis, and proposed that its role is conserved in Staphylococcus aureus.

The results suggest that S. mutans degradosomes are either unlikely to exist or are quite distinct from those of E. coli, andRNase J2 exhibits multiple novel interactions that have not been previously reported for any RNase J proteins, some of which were highly biased for either the cytoplasmic or membrane fractions.

This review will highlight the functional role that BR‐bodies play in the mRNA decay process through its organization into a membraneless organelle in the bacterial cytoplasm, and suggest that these phase‐separated structures are broadly distributed across bacteria, and in evolutionarily related mitochondria and chloroplasts.

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The results suggest that CshA is the functional equivalent of the RhlB helicase of the Escherichia coli RNA degradosome.

RNA degradosome-like complexes appear to be conserved throughout the Proteobacteria, but there is a surprising variability in composition that might contribute to the adaptation of these bacteria to the enormously wide variety of niches in which they live.

The results presented in this work emphasize the importance of RNase Y as the global acting endoribonuclease for B.‚subtilis as well as other Gram‐positive bacteria.

This review focuses on the enzymes and pathways of RNA processing and degradation in Bacillus subtilis, and compares them to those of its gram-negative counterpart, Escherichia coli, to reveal that B. subtili has a very different selection of RNases available for RNA maturation.

RNase Y might be not only important for riboswitch RNA turnover but also as a key player in the initiation of mRNA decay in B. subtilis.

It is shown here that the sequence of the N-terminal endoribonucleolytic domain of RNase E is evolutionarily conserved in Synechocystis sp.

The results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by de gradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of m RNAs for decay by de Gradosomes.

This is the first report demonstrating that RNase E is a membrane‐binding protein and that its localization to the inner cytoplasmic membrane is important for normal cell growth.

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