Localization of components of the RNA-degrading machine in Bacillus subtilis [PDF]
In bacteria, the control of mRNA stability is crucial to allow rapid adaptation to changing conditions. In most bacteria, RNA degradation is catalyzed by the RNA degradosome, a protein complex composed of endo- and exoribonucleases, RNA helicases and ...
Nora Cascante-Estepa+2 more
doaj +3 more sources
Single molecule/particle tracking analysis program SMTracker 2.0 reveals different dynamics of proteins within the RNA degradosome complex inBacillus subtilis [PDF]
Single-molecule (particle) tracking is a powerful method to study dynamic processes in cells at highest possible spatial and temporal resolution. We have developed SMTracker, a graphical user interface for automatic quantifying, visualizing and managing ...
Luis M. Oviedo-Bocanegra+4 more
openalex +2 more sources
The BR-body proteome contains a complex network of protein-protein and protein-RNA interactions [PDF]
Summary: Bacterial ribonucleoprotein bodies (BR-bodies) are non-membrane-bound structures that facilitate mRNA decay by concentrating mRNA substrates with RNase E and the associated RNA degradosome machinery.
Vidhyadhar Nandana+16 more
doaj +2 more sources
The proteomic response to mutants of the Escherichia coli RNA degradosome [PDF]
The Escherichia coli RNA degradosome recognizes and degrades RNA through the coordination of four main protein components, the endonuclease RNase E, the exonuclease PNPase, the RhlB helicase and the metabolic enzyme enolase. To help our understanding of the functions of the RNA degradosome, we quantified expression changes of >2300 proteins using mass ...
Li Zhou+4 more
semanticscholar +4 more sources
Multi-scale ensemble properties of the Escherichia coli RNA degradosome [PDF]
In organisms from all domains of life, multi‐enzyme assemblies play central roles in defining transcript lifetimes and facilitating RNA‐mediated regulation of gene expression.
T. Dendooven+8 more
semanticscholar +6 more sources
RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton [PDF]
RNaseE is the main component of the RNA degradosome of Escherichia coli , which plays an essential role in RNA processing and decay. Localization studies showed that RNaseE and the other known degradosome components (RNA helicase B, polynucleotide phosphorylase, and enolase) are organized as helical filamentous ...
Aziz Taghbalout, Lawrence Rothfield
exaly +5 more sources
Critical functions and key interactions mediated by the RNase E scaffolding domain in Pseudomonas aeruginosa. [PDF]
The RNA degradosome is a bacterial multi-protein complex mediating mRNA processing and degradation. In Pseudomonadota, this complex assembles on the C-terminal domain (CTD) of RNase E through short linear motifs (SLiMs) that determine its composition and
Sandra Amandine Marie Geslain+5 more
doaj +2 more sources
Characterization of Components of the Staphylococcus aureus mRNA Degradosome Holoenzyme-Like Complex [PDF]
ABSTRACTBacterial two-hybrid analysis identified theStaphylococcus aureusRNA degradosome-like complex to include RNase J1, RNase J2, RNase Y, polynucleotide phosphorylase (PNPase), enolase, phosphofructokinase, and a DEAD box RNA helicase. Results also revealed that the recently recognized RNase RnpA interacts with theS. aureusdegradosome and that this
Christelle M. Roux+2 more
semanticscholar +5 more sources
Formation of a membraneless compartment regulates bacterial virulence [PDF]
The RNA-binding protein CsrA regulates the expression of hundreds of genes in several bacterial species, thus controlling virulence and other processes.
Lior Aroeti+11 more
doaj +2 more sources
The endoribonucleolytic N-terminal half of Escherichia coli RNase E is evolutionarily conserved in Synechocystis sp. and other bacteria but not the C-terminal half, which is sufficient for degradosome assembly [PDF]
Escherichia coli RNase E, an essential single-stranded specific endoribonuclease, is required for both ribosomal RNA processing and the rapid degradation of mRNA.
Jakobsen, J.S.+5 more
core +4 more sources