Hervé Menoni
École normale supérieure de Lyon
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Publication
Featured researches published by Hervé Menoni.
The EMBO Journal | 2006
Dimitar Angelov; Vladimir A. Bondarenko; Sébastien Almagro; Hervé Menoni; Fabien Mongelard; Fabienne Hans; Flore Mietton; Vasily M. Studitsky; Ali Hamiche; Stefan Dimitrov; Philippe Bouvet
Remodeling machines play an essential role in the control of gene expression, but how their activity is regulated is not known. Here we report that the nuclear protein nucleolin possesses a histone chaperone activity and that this factor greatly enhances the activity of the chromatin remodeling machineries SWI/SNF and ACF. Interestingly, nucleolin is able to induce the remodeling by SWI/SNF of macroH2A, but not of H2ABbd nucleosomes, which are otherwise resistant to remodeling. This new histone chaperone promotes the destabilization of the histone octamer, helping the dissociation of a H2A–H2B dimer, and stimulates the SWI/SNF‐mediated transfer of H2A–H2B dimers. Furthermore, nucleolin facilitates transcription through the nucleosome, which is reminiscent of the activity of the FACT complex. This work defines new functions for histone chaperones in chromatin remodeling and regulation of transcription and explains how nucleolin could act on transcription.
The EMBO Journal | 2006
Cécile Marie Doyen; Fabien Montel; Thierry Gautier; Hervé Menoni; Cyril Claudet; Marlène Delacour-Larose; Dimitri Angelov; Ali Hamiche; Jan Bednar; Cendrine Faivre-Moskalenko; Philippe Bouvet; Stefan Dimitrov
The histone variant H2A.Bbd appeared to be associated with active chromatin, but how it functions is unknown. We have dissected the properties of nucleosome containing H2A.Bbd. Atomic force microscopy (AFM) and electron cryo‐microscopy (cryo‐EM) showed that the H2A.Bbd histone octamer organizes only ∼130 bp of DNA, suggesting that 10 bp of each end of nucleosomal DNA are released from the octamer. In agreement with this, the entry/exit angle of the nucleosomal DNA ends formed an angle close to 180° and the physico‐chemical analysis pointed to a lower stability of the variant particle. Reconstitution of nucleosomes with swapped‐tail mutants demonstrated that the N‐terminus of H2A.Bbd has no impact on the nucleosome properties. AFM, cryo‐EM and chromatin remodeling experiments showed that the overall structure and stability of the particle, but not its property to interfere with the SWI/SNF induced remodeling, were determined to a considerable extent by the H2A.Bbd docking domain. These data show that the whole H2A.Bbd histone fold domain is responsible for the unusual properties of the H2A.Bbd nucleosome.
Molecular and Cellular Biology | 2007
Hervé Menoni; Didier Gasparutto; Ali Hamiche; Jean Cadet; Stefan Dimitrov; Philippe Bouvet; Dimitar Angelov
ABSTRACT In eukaryotes, base excision repair (BER) is responsible for the repair of oxidatively generated lesions. The mechanism of BER on naked DNA substrates has been studied in detail, but how it operates on chromatin remains unclear. Here we have studied the mechanism of BER by introducing a single 8-oxo-7,8-dihydroguanine (8-oxoG) lesion in the DNA of reconstituted positioned conventional and histone variant H2A.Bbd nucleosomes. We found that 8-oxoguanine DNA glycosylase, apurinic/apyrimidinic endonuclease, and polymerase β activities were strongly reduced in both types of nucleosomes. In conventional nucleosomes SWI/SNF stimulated the processing of 8-oxoG by each one of the three BER repair factors to efficiencies similar to those for naked DNA. Interestingly, SWI/SNF-induced remodeling, but not mobilization of conventional nucleosomes, was required to achieve this effect. A very weak effect of SWI/SNF on the 8-oxoG BER removal in H2A.Bbd histone variant nucleosomes was observed. The possible implications of our data for the understanding of in vivo mechanisms of BER are discussed.
Nucleic Acids Research | 2012
Hervé Menoni; Manu Shubhdarshan Shukla; Véronique Gerson; Stefan Dimitrov; Dimitar Angelov
In this work we have studied the effect of chromatin structure on the base excision repair (BER) efficiency of 8-oxoG. As a model system we have used precisely positioned dinucleosomes assembled with linker histone H1. A single 8-oxoG was inserted either in the linker or the core particle DNA within the dinucleosomal template. We found that in the absence of histone H1 the glycosylase OGG1 removed 8-oxoG from the linker DNA and cleaved DNA with identical efficiency as in the naked DNA. In contrast, the presence of histone H1 resulted in close to 10-fold decrease in the efficiency of 8-oxoG initiation of repair in linker DNA independently of linker DNA length. The repair of 8-oxoG in nucleosomal DNA was very highly impeded in both absence and presence of histone H1. Chaperone-induced uptake of H1 restored the efficiency of the glycosylase induced removal of 8-oxoG from linker DNA, but not from the nucleosomal DNA. We show, however, that removal of histone H1 and nucleosome remodelling are both necessary and sufficient for an efficient removal of 8-oxoG in nucleosomal DNA. Finally, a model for BER of 8-oxoG in chromatin templates is suggested.
Nucleic Acids Research | 2011
Santiago Cuesta-López; Hervé Menoni; Dimitar Angelov; Michel Peyrard
DNA is not the static entity that structural pictures suggest. It has been longly known that it ‘breathes’ and fluctuates by local opening of the bases. Here we show that the effect of structural fluctuations, exhibited by AT-rich low stability regions present in some common transcription initiation regions, influences the properties of DNA in a distant range of at least 10 bp. This observation is confirmed by experiments on genuine gene promoter regions of DNA. The spatial correlations revealed by these experiments throw a new light on the physics of DNA and could have biological implications, for instance by contributing to the cooperative effects needed to assemble the molecular machinery that forms the transcription complex.
Nucleic Acids Research | 2011
Fabien Montel; Martin Castelnovo; Hervé Menoni; Dimitar Angelov; Stefan Dimitrov; Cendrine Faivre-Moskalenko
The ‘remodels structure of chromatin’ (RSC) complex is an essential chromatin remodeling factor that is required for the control of several processes including transcription, repair and replication. The ability of RSC to relocate centrally positioned mononucleosomes at the end of nucleosomal DNA is firmly established, but the data on RSC action on oligo-nucleosomal templates remains still scarce. By using atomic force microscopy (AFM) imaging, we have quantitatively studied the RSC-induced mobilization of positioned di- and trinucleosomes as well as the directionality of mobilization on mononucleosomal template labeled at one end with streptavidin. AFM imaging showed only a limited set of distinct configurational states for the remodeling products. No stepwise or preferred directionality of the nucleosome motion was observed. Analysis of the corresponding reaction pathways allows deciphering the mechanistic features of RSC-induced nucleosome relocation. The final outcome of RSC remodeling of oligosome templates is the packing of the nucleosomes at the edge of the template, providing large stretches of DNA depleted of nucleosomes. This feature of RSC may be used by the cell to overcome the barrier imposed by the presence of nucleosomes.
DNA Repair | 2015
Laura J. Eccles; Hervé Menoni; Dimitar Angelov; Martine E. Lomax; Peter O’Neill
Highlights • Retarded cleavage of abasic site when in nucleosomal DNA by AP endonuclease.• Efficient cleavage of abasic site when in nucleosomal DNA by CHO-K1 nuclear extracts.• Efficient cleavage of bistranded abasic sites in a cluster in nucleosomal DNA by cell extract.• Cleavage of abasic site in bistranded cluster with oxidized guanine in nucleosomal DNA.
PLOS Genetics | 2016
John Lalith Charles Richard; Manu Shubhdarshan Shukla; Hervé Menoni; Khalid Ouararhni; Imtiaz Nisar Lone; Yohan Roulland; Christophe Papin; Elsa Ben Simon; Tapas K. Kundu; Ali Hamiche; Dimitar Angelov; Stefan Dimitrov
FACT, in addition to its role in transcription, is likely implicated in both transcription-coupled nucleotide excision repair and DNA double strand break repair. Here, we present evidence that FACT could be directly involved in Base Excision Repair and elucidate the chromatin remodeling mechanisms of FACT during BER. We found that, upon oxidative stress, FACT is released from transcription related protein complexes to get associated with repair proteins and chromatin remodelers from the SWI/SNF family. We also showed the rapid recruitment of FACT to the site of damage, coincident with the glycosylase OGG1, upon the local generation of oxidized DNA. Interestingly, FACT facilitates uracil-DNA glycosylase in the removal of uracil from nucleosomal DNA thanks to an enhancement in the remodeling activity of RSC. This discloses a novel property of FACT wherein it has a co-remodeling activity and strongly enhances the remodeling capacity of the chromatin remodelers. Altogether, our data suggest that FACT may acts in concert with RSC to facilitate excision of DNA lesions during the initial step of BER.
Molecular Cell | 2017
Jan Bednar; Isabel Garcia-Saez; Amber R. Cutter; Gabor Papai; Anna Reymer; Sajad Hussain Syed; Imtiaz Nisar Lone; Ognyan Tonchev; Corinne Crucifix; Hervé Menoni; Christophe Papin; Dimitrios A. Skoufias; Hitoshi Kurumizaka; Richard Lavery; Ali Hamiche; Jeffrey J. Hayes; Patrick Schultz; Dimitar Angelov; Carlo Petosa; Stefan Dimitrov
Jan Bednar, Isabel Garcia-Saez, Ramachandran Boopathi, Amber R. Cutter, Gabor Papai, Anna Reymer, Sajad H. Syed, Imtiaz Nisar Lone, Ognyan Tonchev, Corinne Crucifix, Hervé Menoni, Christophe Papin, Dimitrios A. Skoufias, Hitoshi Kurumizaka, Richard Lavery, Ali Hamiche,* Jeffrey J. Hayes,* Patrick Schultz,* Dimitar Angelov,* Carlo Petosa,* and Stefan Dimitrov* *Correspondence: [email protected] (A.H.), [email protected] (J.J.H.), [email protected] (P.S.), [email protected] (D.A.), [email protected] (C.P.), [email protected] (S.D.) http://dx.doi.org/10.1016/j.molcel.2017.05.018
Journal of Biochemistry | 2014
Jayasha Shandilya; Parijat Senapati; Fabienne Hans; Hervé Menoni; Philippe Bouvet; Stefan Dimitrov; Dimitar Angelov; Tapas K. Kundu
Mammalian centromeric histone H3 variant, CENP-A, is involved in maintaining the functional integrity and epigenetic inheritance of the centromere. CENP-A causes transcriptional repression of centromeric chromatin through an unknown mechanism. Here, we report that reconstituted CENP-A nucleosomes are amenable to ATP-dependent SWI/SNF-mediated remodelling but are less permissive to acetylation and acetylation-dependent in vitro chromatin transcription. Remarkably, the transcriptional repression of the CENP-A chromatinized template could be relieved by the ectopic addition of histone chaperone, nucleophosmin.