Publications by authors named "A Lecrivain"

Adenosine-to-inosine (A-to-I) RNA editing plays an important role in the post-transcriptional regulation of eukaryotic cell physiology. However, our understanding of the occurrence, function and regulation of A-to-I editing in bacteria remains limited. Bacterial mRNA editing is catalysed by the deaminase TadA, which was originally described to modify a single tRNA in Escherichia coli.

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Article Synopsis
  • RNA degradation is crucial for bacteria to manage gene expression and adapt to different environments, mainly through the actions of endoribonucleases (endoRNases) and exoribonucleases (exoRNases).
  • The study specifically analyzes endoRNase Y and its interaction with three exoRNases in Streptococcus pyogenes, revealing that RNase Y primarily cuts after guanosine to create substrates for the exoRNases.
  • The findings highlight the selective trimming of RNA fragments by PNPase and YhaM after RNase Y processing, demonstrating a novel approach to studying the complex interactions between RNA processing enzymes across the genome.
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Extracellular vesicles (EVs) are released by cells from all kingdoms and represent one form of cell-cell interaction. This universal system of communication blurs cells type boundaries, offering an new avenue for pathogens to infect their hosts. EVs carry with them an arsenal of virulence factors that have been the focus of numerous studies.

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mRNA decay plays an essential role in the control of gene expression in bacteria. Exoribonucleases (exoRNases), which trim transcripts starting from the 5' or 3' end, are particularly important to fully degrade unwanted transcripts and renew the pool of nucleotides available in the cell. While recent techniques have allowed genome-wide identification of ribonuclease (RNase) targets in bacteria in vivo, none of the 3'-to-5' exoRNase targetomes (i.

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Endoribonuclease Y (RNase Y) is a crucial regulator of virulence in Gram-positive bacteria. In the human pathogen Streptococcus pyogenes, RNase Y is required for the expression of the major secreted virulence factor streptococcal pyrogenic exotoxin B (SpeB), but the mechanism involved in this regulation remains elusive. Here, we demonstrate that the 5' untranslated region of speB mRNA is processed by several RNases including RNase Y.

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