Search

Your search keyword '"Loris, Remy"' showing total 785 results
Start Over Author "Loris, Remy"
785 results on '"Loris, Remy"'

12. Structure-Based Design and Synthesis of Stapled 10Panx1 Analogues for Use in Cardiovascular Inflammatory Diseases

Author

Lamouroux, Arthur, primary, Tournier, Malaury, additional, Iaculli, Debora, additional, Caufriez, Anne, additional, Rusiecka, Olga M., additional, Martin, Charlotte, additional, Bes, Viviane, additional, Carpio, Laureano E., additional, Girardin, Yana, additional, Loris, Remy, additional, Tabernilla, Andrés, additional, Molica, Filippo, additional, Gozalbes, Rafael, additional, Mayán, María D., additional, Vinken, Mathieu, additional, Kwak, Brenda R., additional, and Ballet, Steven, additional

Published
2023
Full Text
View/download PDF

18. Structural basis of substrate specificity and neutralization mechanism of the FaRel2/ATfaRel2 toxin-antitoxin system from Coprobacillus sp. D7

Author

Garcia-Pino, Abel, Vanhamme, Luc, Hallet, Bernard, Govaerts, Cédric, Loris, Remy, Perez-Morga, David, Dominguez Molina, Lucia, Garcia-Pino, Abel, Vanhamme, Luc, Hallet, Bernard, Govaerts, Cédric, Loris, Remy, Perez-Morga, David, and Dominguez Molina, Lucia

Abstract

Toxin-antitoxin (TA) systems are widespread in bacterial and archaeal genomes. These TA modulesgenerally encode a toxic component and its cognate antidote in the same operon. In the case of type IITA systems, the antitoxin binds to the toxin to form a nontoxic complex via protein-protein interactionand thus, the toxin is retained in an inactive state protecting the bacterial cells. Under unfavourableconditions in the cell, the TA systems are activated, and the labile antitoxin is degraded by proteases;therefore, the toxin can find its target in the bacterial cell leading to growth inhibition or cell death. Arecent discovery reveals multiple families of small alarmone synthetases (SASs) in which they areencoded in conserved bicistronic architectures that recall toxin-antitoxin modules. ToxSAS (toxicSASs) enzymes act through translation inhibition mediated by pyrophosphorylation of tRNA CCAends, such as FaRel2, or through synthesis of the toxic alarmone (p)ppApp and ATP depletion (such asFaRel). Both enzymatic reactions use ATP as a pyrophosphate donor. In this thesis, we have studiedthe FaRel2 toxSAS effector from Coprobacillus sp. D7 (Coprobacillus) promotes growth arrest in E.coli by inhibiting protein synthesis. FaRel2 transfers a pyrophosphate moiety from ATP to the 3’CCAend of the tRNA. Indeed, this modification abrogates the aminoacylation of tRNA and the starvationsignal of cellular amino acids by the ribosome-RelA enzyme. Virtually nothing is known about theneutralisation mechanism that ATfaRel2 antitoxin exerts to counteract FaRel2 toxicity and diversitytoxicity activity in the new toxSAS subfamilies. In this study, we show that the pseudo-Zn2+ fingerdomain (pZFD) of the ATfaRel2 antitoxin prevents the access of ATP to the pyrophosphate donor siteof the FaRel2 toxin, without affecting the recruitment of the tRNA pyrophosphate acceptor. On thecontrary, toxSASs producing (p)ppApp are inhibited via Tis1 antitoxin domains by occlusion of thepyrophosphate accepto, Doctorat en Sciences, info:eu-repo/semantics/nonPublished

Published
2023

44. Entropic pressure controls olgomerization of Vibrio cholerae ParD2 antitoxin

Author

Garcia Rodriguez, Gabriela, Girardin, Yana, Volkov, Oleksandr, Singh, Ranjan Kumar, Muruganandam, Gopinath, Van Dyck, Jeroen, Sobott, Frank, Versees, Wim, Charlier, Daniel, Loris, Remy, Faculty of Sciences and Bioengineering Sciences, Department of Bio-engineering Sciences, Structural Biology Brussels, and Microbiology

Subjects
Intrinsicallydisordered protein, Oligomer interface, Protein oligomerization, Quaternary structure, structural biology, SAXS, DNA binding, Toxin-Antitoxin module, transcription regulation, X-ray crystallography, Protein-DNA interaction
Abstract

ParD2 is the antitoxin component of the parDE2 toxin-antitoxin module from Vibrio cholerae and consists of an ordered DNA binding domain followed by an intrinsically disordered ParE-neutralizing domain. In absence of the C-terminal IDP domain, VcParD2 crystallizes as a doughnut-shaped hexadecamer formed by the association of eight dimers. This assembly is stabilized via hydrogen bonds and salt bridges rather than hydrophobic contacts. In solution, oligomerization of the full-length protein is restricted to a stable, open 10-mer or 12-mer, likely as a consequence of entropic pressure from the IDP tails. The relative positioning of successive VcParD2 dimers mimics the arrangement of Streptococcus agalactiae CopG dimers on their operator and allows for an extended operator to wrap around the VcParD2 oligomer.

Published
2021
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results