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Jacques Côté

Researcher at Laval University

Publications -  160
Citations -  21037

Jacques Côté is an academic researcher from Laval University. The author has contributed to research in topics: Chromatin & Histone. The author has an hindex of 66, co-authored 149 publications receiving 19330 citations. Previous affiliations of Jacques Côté include Howard Hughes Medical Institute & Pennsylvania State University.

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Primers for mitochondrial DNA replication generated by endonuclease G

TL;DR: The cleavage sites match those found in vivo, indicating that Endo G is capable of generating the RNA primers required by DNA polymerase gamma to initiate replication of mitochondrial DNA.
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Yeast Enhancer of Polycomb defines global Esa1-dependent acetylation of chromatin

TL;DR: Results indicate that the essential aspect of Esa1 and Epl1 resides in picNuA4 function, and propose that picNUA4 represents a nontargeted histone H4/H2A acetyltransferase activity responsible for global acetylation, whereas the NuA4 complex is recruited to specific genomic loci to perturb locally the dynamic acetylated/deacetylation equilibrium.
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Histone Chaperones: Modulators of Chromatin Marks

TL;DR: Novel and striking links that have been established between these proteins and posttranslational modifications of histones are highlighted and how cell memory may be maintained through epigenetic mechanisms involving histone chaperones is discussed.
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Interplay of Chromatin Modifiers on a Short Basic Patch of Histone H4 Tail Defines the Boundary of Telomeric Heterochromatin

TL;DR: It is shown that histone H4 N-terminal domain, unlike other histone tails, interacts with Dot1 and is essential for H3 K79 methylation, and that the heterochromatin protein Sir3 inhibits Dot1-mediated methylation and that this inhibition is dependent on lysine 16 of H4.
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Comprehensive Mapping of Histone Modifications at DNA Double-Strand Breaks Deciphers Repair Pathway Chromatin Signatures

TL;DR: This study revealed the existence of a DSB-induced monoubiquitination-to-acetylation switch on histone H2B lysine 120, likely mediated by the SAGA complex, as well as higher-order signaling at HR-repaired DSBs whereby hist one H1 is evicted while ubiquitin and 53BP1 accumulate over the entire γH2AX domains.