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dc.date.accessioned 2020-05-26T14:07:48Z
dc.date.available 2020-05-26T14:07:48Z
dc.date.issued 2018-05
dc.identifier.uri http://sedici.unlp.edu.ar/handle/10915/96676
dc.description.abstract Subtilases (SBTs) are serine peptidases that are found in all three domains of life. As compared with homologs in other Eucarya, plant SBTs are more closely related to archaeal and bacterial SBTs, with which they share many biochemical and structural features. However, in the course of evolution, functional diversification led to the acquisition of novel, plant-specific functions, resulting in the present-day complexity of the plant SBT family. SBTs are much more numerous in plants than in any other organism, and include enzymes involved in general proteolysis as well as highly specific processing proteases. Most SBTs are targeted to the cell wall, where they contribute to the control of growth and development by regulating the properties of the cell wall and the activity of extracellular signaling molecules. Plant SBTs affect all stages of the life cycle as they contribute to embryogenesis, seed development and germination, cuticle formation and epidermal patterning, vascular development, programmed cell death, organ abscission, senescence, and plant responses to their biotic and abiotic environments. In this article we provide a comprehensive picture of SBT structure and function in plants. en
dc.format.extent 901-915 es
dc.language en es
dc.subject Cell death es
dc.subject Peptide signaling es
dc.subject Plant defense es
dc.subject Plant development es
dc.subject Precursor processing es
dc.subject Proteolysis es
dc.subject Structure–function relationship es
dc.subject Subtilisin-like proteinase es
dc.title From structure to function – a family portrait of plant subtilases en
dc.type Articulo es
sedici.identifier.uri https://ri.conicet.gov.ar/11336/65278 es
sedici.identifier.uri https://nph.onlinelibrary.wiley.com/doi/full/10.1111/nph.14582 es
sedici.identifier.other https://dx.doi.org/10.1111/nph.14582 es
sedici.identifier.other hdl:11336/65278 es
sedici.identifier.issn 0028-646X es
sedici.creator.person Schaller, Andreas es
sedici.creator.person Stintzi, Annick es
sedici.creator.person Rivas, Susana es
sedici.creator.person Serrano, Irene es
sedici.creator.person Chichkova, Nina V. es
sedici.creator.person Vartapetian, Andrey B. es
sedici.creator.person Martínez, Dana Ethel es
sedici.creator.person Guiamet, Juan José es
sedici.creator.person Sueldo, Daniela Jorgelina es
sedici.creator.person van der Hoorn, Renier A. L. es
sedici.creator.person Ramírez, Vicente es
sedici.creator.person Vera, Pablo es
sedici.subject.materias Biología es
sedici.subject.materias Ciencias Naturales es
sedici.subject.materias Ciencias Exactas es
sedici.description.fulltext true es
mods.originInfo.place Instituto de Fisiología Vegetal es
sedici.subtype Articulo es
sedici.rights.license Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Argentina (CC BY-NC-SA 2.5)
sedici.rights.uri http://creativecommons.org/licenses/by-nc-sa/2.5/ar/
sedici.description.peerReview peer-review es
sedici.relation.journalTitle New Phytologist es
sedici.relation.journalVolumeAndIssue vol. 218, no. 3 es


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Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Argentina (CC BY-NC-SA 2.5) Excepto donde se diga explícitamente, este item se publica bajo la siguiente licencia Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Argentina (CC BY-NC-SA 2.5)