Function and architecture
of macromolecular assemblies
Principal Investigators: Sophie Quevillon-Cheruel, Stéphanie Marsin and Hélène Walbott
Engineers involved: Inès Li de la Sierra-Gallay and Magali Aumont-Nicaise
PhD involved: Claire Cargemel
Study of DnaB•DciA reveals insights into the primary mode of loading of the bacterial replicative helicase
Marsin S, Adam Y, Cargemel C, Andreani J, Baconnais S, Legrand P, Gallay-Li de la Sierra I, Humbert A, Aumont-Nicaise M, Velours C, Ochsenbein F, Durand D, Le Cam E, Walbott H, Possoz C, Quevillon-Cheruel S, Ferat JL
Chan-Yao-Chong et al. (2020) J Struct Biol. 212:107573.
Brézellec et al. (2016) Nat Commun. 7:13271.
Principal Investigator: Sylvie Nessler
Ingeneers involved: Noureddine Lazar, Inès Li de la Sierra-Gallay
Former students involved: Rosa Granha, Samira Zouhir, Antoine Talagas, Jordhan Thuillier
Ledesma-Garcia et al. (2020) Proc Natl Acad Sci USA. 117:7745-7754
Mignolet et al. (2019) eLife 8: e47139
Talagas et al. (2016) PLoS Pathog. 12:e1005980
Shanker et al. (2016) PLoS Pathog. 12:e1005979
Perchat et al. (2016) Microb Cell. 3:573-575
Perchat et al. (2016) PLoS Pathog. 12:e1005779
Zouhir et al. (2013) Nucleic Acids Res. 41:7920-33
Dubois et al. (2013) Mol Microbiol. 88: 48-63
Grenha et al. (2013) Proc Natl Acad Sci USA. 110: 1047-52
Perchat et al. (2011) Mol Microbiol. 82: 619-633
Principal investigators : Herman van Tilbeurgh, Dominique Liger & Bruno Collinet
Kopina et al. (2021) Nucleic Acids Res. 49:2141–2160
Arrondel et al. (2019) Nat Commun. 10:3967.
Braun et al. (2017) Nat Genet. 49:1529-1538.
Missoury et al. (2018) Nucleic Acids Res. 46:5850-5860
Zhang et al. (2015) Nucleic Acids Res. 43: 3358–3372.
Zhang et al. (2015) Nucleic Acids Res. 43:1804-1817.
Perrochia et al. (2013) Nucleic Acids Res. 41:1953-1964.
Daugeron et al. (2011) Nucleic Acids Res. 39:6148-6160.
Hecker et al. (2008) EMBO J. 27:2340-2351.
Hecker et al. (2007) Nucleic Acids Res. 35:6042-6051.
Team members involved: Ines Gallay, Noureddine Lazar & Herman van Tilbeurgh
Ma et al. (2017) Nucleic Acids Res. 45:6209-6216.
Ma et al. (2017) Biochem J. 474:3599-3613.
Pellegrini et al. (2012) Structure. 20:1769-1777.
Graille et al. (2006) J Biol Chem.;281:30175-85.
Li de la Sierra-Gallay et al. (2005) Nature 433:657-661.
The Leptosphaeria maculans ascomycete fungus is the causal agent of one of the most devastating colza.
During infection, the Leptosphaeria maculans pathogen secretes an arsenal of small proteins (SSPs) or effectors, capable of modulating the response or immunity of the plant and of facilitating fungus infection. Some of these effectors, called avirulence effectors (AVR); are involved in a specific response of the plant against the infection (ETI for effector triggered immunity). The AVR proteins are targeted by plant resistance proteins (R). The avirulence proteins are usually small cysteine rich proteins that do not display sequence homologies with other proteins and hence their biochemical function is therefore difficult to predict. Also, their interactions (direct or indirect) with plant target proteins are poorly understood. The 3D structure determination of the avirulence effectors has proven to be instrumental for the comprehension of their biological function. We combine structural and biochemical approaches to study the avirulence effector AvrLm4-7 (Blondeau, Blaise et al., 2015). A few more effector protein structures have been determined since, using procaryotic or eukaryotic expression systems. These structures were very informative on the mutual functional relationships of these effectors. A new project has been initiated to study the interactions of these effectors with their resistance and or target plant proteins.
Lazar et al. (2021) bioRxiv.12.17.423041
Berny et al. (2020) Front. Bioeng. Biotechnol. 8:16
Blondeau et al. (2015) Plant J. 83:610–624.
Taveneau et al. (2015) Protein Expr Purif. 114:121-127
Hmida-Sayari et al. (2014) Mol. Biotechnol. 56: 839-848
Tiouajni et al. (2014) FEBS J. 281:5513-31.