The news correspondents obtained a quote from the research, "The latter appear as extended cytoplasmic membrane-associated assemblies that coil around the periphery of the cell when visualized by immunofluorescence microscopy. The co-localizing ensemble of RNA metabolic proteins includes RNaseE, PNPase (polynucleotide phosphorylase), the DEAD-box RNA helicase RhlB, the oligo-RNase Orn, RNases II and III, PAP I [poly(A) polymerase I], RppH (RNA pyrophosphohydrolase), proteins RraA and RraB that are negative regulators of RNaseE, and the RNA chaperone Hfq. Not all cellular RNA-binding proteins associate with these structures, as shown for EF-Tu (elongation factor Tu) and Rho helicase. Formation of the supramolecular architecture was shown to not be dependent on two other known cytoskeletal systems or on RNA de novo synthesis or nucleoid positioning within the cell."
According to the news reporters, the research concluded: "This novel dimension of compartmentalization in bacteria that lack classic cell compartments opens new perspectives on how RNA homoeostasis is achieved, organized and regulated in bacteria such as E."
For more information on this research see: Supramolecular membrane-associated assemblies of RNA metabolic proteins in Escherichia coli.
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