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dc.contributor.author
Weisslocker-Schaetzel, Marine
dc.contributor.author
André, François
dc.contributor.author
Touazi, Nabila
dc.contributor.author
Foresi, Noelia Pamela
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Lembrouk, Mehdi
dc.contributor.author
Dorlet, Pierre
dc.contributor.author
Frelet Barrand, Annie
dc.contributor.author
Lamattina, Lorenzo
dc.contributor.author
Santolini, Jérôme
dc.date.available
2018-11-28T14:56:50Z
dc.date.issued
2017-12
dc.identifier.citation
Weisslocker-Schaetzel, Marine; André, François; Touazi, Nabila; Foresi, Noelia Pamela; Lembrouk, Mehdi; et al.; The NOS-like protein from the microalgae Ostreococcus tauri is a genuine and ultrafast NO-producing enzyme; Elsevier Ireland; Plant Science; 265; 12-2017; 100-111
dc.identifier.issn
0168-9452
dc.identifier.uri
http://hdl.handle.net/11336/65421
dc.description.abstract
The exponential increase of genomes’ sequencing has revealed the presence of NO-Synthases (NOS) throughout the tree of life, uncovering an extraordinary diversity of genetic structure and biological functions. Although NO has been shown to be a crucial mediator in plant physiology, NOS sequences seem present solely in green algae genomes, with a first identification in the picoplankton species Ostreococcus tauri. There is no rationale so far to account for the presence of NOS in this early-diverging branch of the green lineage and its absence in land plants. To address the biological function of algae NOS, we cloned, expressed and characterized the NOS oxygenase domain from Ostreococcus tauri (OtNOSoxy). We launched a phylogenetic and structural analysis of algae NOS, and achieved a 3D model of OtNOSoxy by homology modeling. We used a combination of various spectroscopies to characterize the structural and electronic fingerprints of some OtNOSoxy reaction intermediates. The analysis of OtNOSoxy catalytic activity and kinetic efficiency was achieved by stoichiometric stopped-flow. Our results highlight the conserved and particular features of OtNOSoxy structure that might explain its ultrafast NO-producing capacity. This integrative Structure-Catalysis-Function approach could be extended to the whole NOS superfamily and used for predicting potential biological activity for any new NOS.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Ireland
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Algae
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Catalysis
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Function
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No Synthase
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Plant
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Structure
dc.subject.classification
Otras Ciencias Biológicas
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
The NOS-like protein from the microalgae Ostreococcus tauri is a genuine and ultrafast NO-producing enzyme
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-10-23T14:12:22Z
dc.journal.volume
265
dc.journal.pagination
100-111
dc.journal.pais
Irlanda
dc.journal.ciudad
Shannon
dc.description.fil
Fil: Weisslocker-Schaetzel, Marine. Université Paris Sud; Francia
dc.description.fil
Fil: André, François. Université Paris Sud; Francia
dc.description.fil
Fil: Touazi, Nabila. Université Paris Sud; Francia
dc.description.fil
Fil: Foresi, Noelia Pamela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
dc.description.fil
Fil: Lembrouk, Mehdi. Université Paris Sud; Francia
dc.description.fil
Fil: Dorlet, Pierre. Université Paris Sud; Francia
dc.description.fil
Fil: Frelet Barrand, Annie. Université Paris Sud; Francia
dc.description.fil
Fil: Lamattina, Lorenzo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
dc.description.fil
Fil: Santolini, Jérôme. Université Paris Sud; Francia
dc.journal.title
Plant Science
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1016/j.plantsci.2017.09.019
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0168945217303783
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