Pascal Dumoulin
Centre national de la recherche scientifique
6 Papers
93 Citations
Pascal Dumoulin is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Repressor & Repressor lexA. The author has an hindex of 6, co-authored 6 publications.
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Papers
A model for the LexA repressor DNA complex
R. M. A. Knegtel,Rasmus H. Fogh,G. Ottleben,Heinz Rüterjans,Pascal Dumoulin,Manfred Schnarr,Rolf Boelens,Robert Kaptein +7 more
TL;DR: A structural model for the interaction of the LexA repressor DNA binding domain (DBD) with operator DNA is derived by means of Monte Carlo docking and a large number of nonspecific interactions between protein and DNA is observed.
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Structure of the LexA repressor-DNA complex probed by affinity cleavage and affinity photo-cross-linking.
Pascal Dumoulin,Richard H. Ebright,R. M. A. Knegtel,Robert Kaptein,Michèle Granger-Schnarr,Manfred Schnarr +5 more
TL;DR: The structure of the complex of full-length Escherichia coli LexA repressor with a consensus operator DNA fragment has been probed by affinity photo-cross-linking and affinity cleavage to define the orientation of the LexA DNA binding domain relative to the operator and provide support for the model of theLexA-operator complex proposed by Knegtel et al.
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Functional analysis of six genes from chromosomes XIV and XV of Saccharomyces cerevisiae reveals YOR145c as an essential gene and YNL059c/ARP5 as a strain-dependent essential gene encoding nuclear proteins
TL;DR: Basic functional analysis of strains deleted for six open reading frames revealed that deletion of YNL059c/ARP5 was lethal for vegetative growth in strain W303 and caused severe growth defects in strain FY1679 while YOR145c was essential for growth in both strains.
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Orientation of the LexA DNA-binding motif on operator DNA as inferred from cysteine-mediated phenyl azide crosslinking.
TL;DR: It is shown that LexA-C52* may be selectively photocrosslinked with two adjacent bases within each operator half-site, which implies that the LexA recognition helix is oriented opposite to what is generally observed for helix-turn-helix proteins.
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The Saccharomyces cerevisiae Homologue of Human Wiskott–Aldrich Syndrome Protein Las17p Interacts with the Arp2/3 Complex
Ammar Madania,Pascal Dumoulin,Sandrine Grava,Hiroko Kitamoto,Claudia Schärer-Brodbeck,Alexandre Soulard,Violaine Moreau,Barbara Winsor +7 more
TL;DR: Two hybrid results suggest that Las17p interacts with actin, verprolin, Rvs167p and several other proteins including Src homology 3 (SH3) domain proteins, suggesting thatLas17p may integrate signals from different regulatory cascades destined for the Arp2/3p complex and the actin cytoskeleton.