News Column

Studies from P.G. Hoch et al Add New Findings in the Area of Peptides and Proteins

May 20, 2014

By a News Reporter-Staff News Editor at Life Science Weekly -- Research findings on Peptides and Proteins are discussed in a new report. According to news reporting from Marburg, Germany, by NewsRx journalists, research stated, "Controlled RNA degradation is known to be achieved via the exosome in Eukarya and Archaea, and the RNA degradosome in Bacteria. In this issue of the Biochemical Journal, Taghbalout et al. demonstrate in Escherichia coli that many additional proteins of the RNA degradation and processing network co-localize with the RNA degradosome in supramolecular structures."

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. The Biochemical Journal, 2014;458(1):e1-3 (see also Peptides and Proteins).

Our news journalists report that additional information may be obtained by contacting P.G. Hoch, *Institut fur Pharmazeutische Chemie, Philipps-Universitat Marburg, Marbacher Weg 6, 35037 Marburg, Germany.

Keywords for this news article include: Europe, Marburg, Germany, Amino Acids, Nanotechnology, Supramolecular, Escherichia coli, Enterobacteriaceae, Emerging Technologies, Peptides and Proteins, Gram Negative Bacteria.

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Source: Life Science Weekly

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