Publications by authors named "J P Letoquart"
Context: Abdominal trauma (AT) appears to be frequent in Haiti, which is confronted with recurrent socio-political violence.
Objective: To study patients admitted for AT to the Médecins Sans Frontières (MSF) Tabarre trauma centre (Port-au-Prince), and the circumstances of occurrence.
Design: This was a cross-sectional study with retrospective data from January 2020 to December 2021.
OmpA, a protein commonly found in the outer membrane of Gram-negative bacteria, has served as a paradigm for the study of β-barrel proteins for several decades. In , OmpA was previously reported to form complexes with RcsF, a surface-exposed lipoprotein that triggers the Rcs stress response when damage occurs in the outer membrane and the peptidoglycan. How OmpA interacts with RcsF and whether this interaction allows RcsF to reach the surface has remained unclear.
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- The BAM machinery is essential for inserting outer membrane β-barrel proteins (OMPs) in Gram-negative bacteria, and it also helps export the stress sensor RcsF to the cell surface.
- The study reveals the crystal structure of BamA in a complex with RcsF, showing that BamA has a closed lateral gate while RcsF is located deep within its barrel.
- The researchers propose a "push-and-pull" model for how RcsF is exported via BamA, suggesting that the interaction helps RcsF sense envelope stress and that the flow of incoming OMPs regulates BAM activity.
Article Synopsis
- Protein synthesis is a complex process that involves various protein factors and nucleic acids, requiring multiple maturation steps like post-transcriptional and post-translational modifications.
- In eukaryotes, the protein Trm112 activates several methyltransferases involved in targeting different translation machinery components, including rRNA and tRNAs.
- Study of Trm112 in the archaeon Haloferax volcanii reveals a more intricate interaction network than expected, showing similarities with both eukaryotic and bacterial methyltransferases, highlighting its essential role across all domains of life.
-threonyl-carbamoyl adenosine (tA) is a universal tRNA modification found at position 37, next to the anticodon, in almost all tRNAs decoding ANN codons (where N = A, U, G, or C). tA stabilizes the codon-anticodon interaction and hence promotes translation fidelity. The first step of the biosynthesis of tA, the production of threonyl-carbamoyl adenylate (TC-AMP), is catalyzed by the Sua5/TsaC family of enzymes.
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