The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited.

Autor: Mounia Lahfa, Philippe Barthe, Karine de Guillen, Stella Cesari, Mouna Raji, Thomas Kroj, Marie Le Naour-Vernet, François Hoh, Pierre Gladieux, Christian Roumestand, Jérôme Gracy, Nathalie Declerck, André Padilla

Publikováno v: PLoS Pathogens, Vol 20, Iss 5, p e1012176 (2024)

Magnaporthe AVRs and ToxB-like (MAX) effectors constitute a family of secreted virulence proteins in the fungus Pyricularia oryzae (syn. Magnaporthe oryzae), which causes blast disease on numerous cereals and grasses. In spite of high sequence diverg

Externí odkaz: https://doaj.org/article/05ba20d0e9b1499aaf7604f2e1ef2251

Does a Similar 3D Structure Mean a Similar Folding Pathway? The Presence of a C-Terminal α-Helical Extension in the 3D Structure of MAX60 Drastically Changes the Folding Pathway Described for Other MAX-Effectors from Magnaporthe oryzae

Autor: Mounia Lahfa, Assia Mouhand, Karine de Guillen, Philippe Barthe, Thomas Kroj, André Padilla, Christian Roumestand

Publikováno v: Molecules, Vol 28, Iss 16, p 6068 (2023)

Does a similar 3D structure mean a similar folding pathway? This question is particularly meaningful when it concerns proteins sharing a similar 3D structure, but low sequence identity or homology. MAX effectors secreted by the phytopathogenic fungus

Externí odkaz: https://doaj.org/article/4c4e5950cfbc46a188bf10f7ec703668

Structure Analysis Uncovers a Highly Diverse but Structurally Conserved Effector Family in Phytopathogenic Fungi.

Autor: Karine de Guillen, Diana Ortiz-Vallejo, Jérome Gracy, Elisabeth Fournier, Thomas Kroj, André Padilla

Publikováno v: PLoS Pathogens, Vol 11, Iss 10, p e1005228 (2015)

Phytopathogenic ascomycete fungi possess huge effector repertoires that are dominated by hundreds of sequence-unrelated small secreted proteins. The molecular function of these effectors and the evolutionary mechanisms that generate this tremendous n

Externí odkaz: https://doaj.org/article/c8a92c60cecf439e84e207741966a6f2

Combining High-Pressure NMR and Geometrical Sampling to Obtain a Full Topological Description of Protein Folding Landscapes: Application to the Folding of Two MAX Effectors from Magnaporthe oryzae

Autor: Cécile Dubois, Mounia Lahfa, Joana Pissarra, Karine de Guillen, Philippe Barthe, Thomas Kroj, Christian Roumestand, André Padilla

Publikováno v: International Journal of Molecular Sciences
International Journal of Molecular Sciences, 2022, 23 (10), pp.5461. ⟨10.3390/ijms23105461⟩
International Journal of Molecular Sciences; Volume 23; Issue 10; Pages: 5461

International audience; Despite advances in experimental and computational methods, the mechanisms by which an unstructured polypeptide chain regains its unique three-dimensional structure remains one of the main puzzling questions in biology. Single

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::814eb776bcead070c4296fb0d6d8a972
https://hal.science/hal-03705665/document

Structure Structural insights into the allosteric activation of the LicT antiterminator by PTS- mediated phosphorylation

Autor: Yinshan Yang, ANDRE PADILLA, Karine de Guillen, Léa Mammri, Jérôme Gracy, Nathalie Declerck, Héléne Démèné

Publikováno v: Structure
Structure, Elsevier (Cell Press), 2020, 28 (2), pp.244-251.e3. ⟨10.1016/j.str.2019.10.017⟩
HAL

International audience; LicT belongs to an essential family of bacterial transcriptional antitermination proteins controlling the expression of sugar-metabolizing operons. When activated, they bind to nascent mRNAs, preventing premature arrest of tra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::f5ac279d2c1f29f9e1c2b38dd135555a
https://hal.archives-ouvertes.fr/hal-02368196/file/STRUCTURE-D-18-00254_R4.pdf