Gaëlle Batot
University of Utah
11 Papers
32 Citations
Gaëlle Batot is an academic researcher from University of Utah. The author has contributed to research in topics: Phosphorylation & Kinase. The author has an hindex of 5, co-authored 10 publications. Previous affiliations of Gaëlle Batot include University of Auckland & University of Dundee.
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Papers
Crystal structures of Burkholderia cenocepacia dihydropteroate synthase in the apo-form and complexed with the product 7,8-dihydropteroate
Rachel E. Morgan,Gaëlle Batot,Jennifer M Dement,Vincenzo A. Rao,Thomas C. Eadsforth,William N. Hunter +5 more
TL;DR: Structural similarities between Bc DHPS and orthologues from other Gram-negative species are evident as expected on the basis of a high level of sequence identity and provide a foundation for hit discovery.
The CDI toxin of Yersinia kristensenii is a novel bacterial member of the RNase A superfamily.
Gaëlle Batot,Karolina Michalska,Greg Ekberg,Ervin M Irimpan,Grazyna Joachimiak,Robert Jedrzejczak,Gyorgy Babnigg,Christopher S. Hayes,Andrzej Joachimiak,Andrzej Joachimiak,Celia W. Goulding +10 more
TL;DR: CdiA-CTYkris is the first non-vertebrate protein found to possess the RNase A superfamily fold, and homologs of this toxin are associated with secretion systems in many Gram-negative and Gram-positive bacteria, suggesting thatRNase A-like toxins are commonly deployed in inter-bacterial competition.
Peptide binding to a bacterial signal peptidase visualized by peptide tethering and carrier-driven crystallization.
Yi Tian Ting,Paul W. R. Harris,Gaëlle Batot,Margaret A. Brimble,Edward N. Baker,Paul G. Young +5 more
TL;DR: Utilizing a peptide-anchoring strategy, transient signal-peptide complexes of a Gram-positive bacterial signal peptidase were trapped, revealing the atomic details of their interaction.
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Selective kinase inhibition shows that Bur1 (Cdk9) phosphorylates the Rpb1 linker in vivo
Yujin Chun,Hyunsuk Suh,Yoo Jin Joo,Gaëlle Batot,Christopher P. Hill,Tim Formosa,Stephen Buratowski +6 more
TL;DR: Phosphorylation of the Rpb1 linker enhances binding of the Spt6 tSH2 domain, and here it is shown that Bur1/Cdk9 is the kinase responsible for this modification in vivo.
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Alteration of fluorescent protein spectroscopic properties upon cryoprotection.
David von Stetten,Gaëlle Batot,Marjolaine Noirclerc-Savoye,Marjolaine Noirclerc-Savoye,Antoine Royant +4 more
TL;DR: The spectroscopic and structural effects of the two cryoprotectants glycerol and ethylene glycol on the cyan fluorescent protein Cerulean were investigated and showed a systematic red shift of the UV-vis absorption and fluorescence emission spectra, reinforcing the notion that fluorescent proteins must not been seen as rigid structures.
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