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Chloe Zubieta
Researcher at University of Grenoble
Publications - 90
Citations - 4756
Chloe Zubieta is an academic researcher from University of Grenoble. The author has contributed to research in topics: Gene & Transcription factor. The author has an hindex of 28, co-authored 82 publications receiving 3738 citations. Previous affiliations of Chloe Zubieta include Salk Institute for Biological Studies & Hoffmann-La Roche.
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Journal ArticleDOI
A circRNA from SEPALLATA3 regulates splicing of its cognate mRNA through R-loop formation
Vanessa M. Conn,Vanessa M. Conn,Véronique Hugouvieux,Aditya Nayak,Stephanie A. Conos,Giovanna Capovilla,Gökhan Cildir,Agnès Jourdain,Vinay Tergaonkar,Vinay Tergaonkar,Vinay Tergaonkar,Markus Schmid,Markus Schmid,Chloe Zubieta,Simon J. Conn,Simon J. Conn +15 more
TL;DR: It is reported that circRNAs can be used as bona fide biomarkers of functional, exon-skipped AS variants in Arabidopsis, including in the homeotic MADS-box transcription factor family and provides the first evidence of an organismal-level phenotype mediated by circRNA manipulation.
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Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases.
TL;DR: These two OMTs constitute the first plant methyltransferases to be structurally characterized and reveal a novel oligomerization domain and the molecular determinants for substrate selection and this work provides a structural basis for understanding the substrate specificity of the diverse family of plant O MTs and facilitates the engineering of novel activities in this extensive class of natural product biosynthetic enzymes.
Journal ArticleDOI
Cooperative Assembly of TGF-β Superfamily Signaling Complexes Is Mediated by Two Disparate Mechanisms and Distinct Modes of Receptor Binding
Jay C. Groppe,Cynthia S. Hinck,Payman Samavarchi-Tehrani,Chloe Zubieta,Jonathan P. Schuermann,Alexander B. Taylor,Patricia M. Schwarz,Jeffrey L. Wrana,Andrew P. Hinck +8 more
TL;DR: The crystal structure of TGF-beta3 in complex with the extracellular domains of both pairs of receptors is reported, revealing that the type I docks and becomes tethered via unique extensions at a composite ligand-type II interface.
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A prion-like domain in ELF3 functions as a thermosensor in Arabidopsis.
Jaehoon Jung,Jaehoon Jung,Antonio Daniel Barbosa,Stephanie Hutin,Janet R. Kumita,Mingjun Gao,Dorothee Derwort,Catarina S. Silva,Xuelei Lai,Xuelei Lai,Elodie Pierre,Feng Geng,Sol-Bi Kim,Sujeong Baek,Chloe Zubieta,Katja E. Jaeger,Katja E. Jaeger,Philip A. Wigge,Philip A. Wigge,Philip A. Wigge +19 more
TL;DR: It is shown that ELF3 proteins in plants from hotter climates, with no detectable PrD, are active at high temperatures, and lack thermal responsiveness, which represents a previously unknown thermosensory mechanism.
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Arabidopsis Isochorismate Synthase Functional in Pathogen-induced Salicylate Biosynthesis Exhibits Properties Consistent with a Role in Diverse Stress Responses
TL;DR: The biochemical properties of AtICS1 indicate its activity is not regulated by light-dependent changes in stromal pH, Mg2+, or redox and that it is remarkably active at 4 °C consistent with a role for SA in cold-tolerant growth.