Dr. Nourani holds a PhD from the Pierre et Marie Curie University (Paris VI). He joined the Quebec CRCHU in July 2005, following a postdoctoral fellowship in the Department of Genetics at Harvard Medical School in Boston. Dr. Nourani has held a Canada Research Chair, from 2007 to 2017, whose primary goal is to study the regulation mechanisms of gene transcription. He is currently a Professor in the Department of Molecular Biology, Medical Biochemistry and Pathology of the Faculty of Medicine of Laval University.
The smooth functioning of cells depends on their ability to respond and adapt to extracellular changes. A large part of adaptive responses is to activate or repress gene expression, usually at the transcriptional level. A defect in transcriptional responses to external stimuli may result in uncontrolled proliferation or aberrant differentiation leading to the development of cancers.
To understand the regulation of transcription, we cannot ignore the dynamic role of chromatin. It allows for the condensation of eukaryotic genomes in the nucleus and plays a crucial role in gene transcription. The basic unit of chromatin, the nucleosome, strongly inhibits several steps leading to the production of transcripts. Our research program is based on the assumption that the movement of the ARNP II produces a profound alteration of the chromatin structure. To meet these constraints, cells have developed adaptive mechanisms to repair this damage. Deficiency in this function results in aberrant transcription initiation, erroneous regulation, and genome instability. Our goal is to improve the general understanding of the mechanisms implemented by the cell to rebuild, in the wake of the ARNP II, an adequate chromatin structure. Dr. Nourani’s work is based on genetic, biochemical and genomic approaches in different model organisms. The purpose of this research is to improve the general knowledge of the functioning of our cells. Its short-term goal is to dissect the mechanisms of epigenetic regulation of genes.
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- Gamar, LyndaEmployeeL'Hôtel-Dieu de Québec+1 418-525-4444, extension 16898+1 418-691-5439Lynda.Gamar@crchudequebec.ulaval.ca
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- Rufiange, AnneEmployeeL'Hôtel-Dieu de Québec+1 418-525-4444, extension 16898+1 firstname.lastname@example.org
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Casein kinase 2 mediated phosphorylation of Spt6 modulates histone dynamics and regulates spurious transcription.Journal Article
Nucleic Acids Res, 46 (15), pp. 7612-7630, 2018, ISSN: 0305-1048.
Structure-function studies of histone H3/H4 tetramer maintenance during transcription by chaperone Spt2.Journal Article
Genes Dev, 29 (12), pp. 1326-40, 2015, ISSN: 0890-9369.
Eaf5/7/3 form a functionally independent NuA4 submodule linked to RNA polymerase II-coupled nucleosome recycling.Journal Article
EMBO J, 33 (12), pp. 1397-415, 2014, ISSN: 0261-4189.
Casein kinase 2 associates with the yeast chromatin reassembly factor Spt2/Sin1 to regulate its function in the repression of spurious transcription.Journal Article
Mol Cell Biol, 33 (21), pp. 4198-211, 2013, ISSN: 0270-7306.
Histone chaperones: modulators of chromatin marks.Journal Article
Mol Cell, 41 (5), pp. 502-14, 2011, ISSN: 1097-2765.
Transcription regulation by the noncoding RNA SRG1 requires Spt2-dependent chromatin deposition in the wake of RNA polymerase II.Journal Article
Mol Cell Biol, 31 (6), pp. 1288-300, 2011, ISSN: 0270-7306.
The Rtt106 histone chaperone is functionally linked to transcription elongation and is involved in the regulation of spurious transcription from cryptic promoters in yeast.Journal Article
J Biol Chem, 283 (41), pp. 27350-4, 2008, ISSN: 0021-9258.
Eaf1 is the platform for NuA4 molecular assembly that evolutionarily links chromatin acetylation to ATP-dependent exchange of histone H2A variants.Journal Article
Mol Cell Biol, 28 (7), pp. 2257-70, 2008, ISSN: 0270-7306.
Evidence that the localization of the elongation factor Spt16 across transcribed genes is dependent upon histone H3 integrity in Saccharomyces cerevisiae.Journal Article
Genetics, 177 (1), pp. 101-12, 2007, ISSN: 0016-6731.
Genome-wide replication-independent histone H3 exchange occurs predominantly at promoters and implicates H3 K56 acetylation and Asf1.Journal Article
Mol Cell, 27 (3), pp. 393-405, 2007, ISSN: 1097-2765.