Cysteine-proteases and cystatins from barley: molecular and functional characterization in housekeeping and defense processes

Martinez Muñoz, Manuel; Cambra Marin, Ines; Gonzalez-Melendi de Leon, Pablo; Santamaria, Maria E. y Diaz Rodriguez, Isabel (2011). Cysteine-proteases and cystatins from barley: molecular and functional characterization in housekeeping and defense processes. En: "1st International conference on PLANT PROTEASES", 10/04/2011 - 14/04/2011, Hemava, Suecia.

Descripción

Título: Cysteine-proteases and cystatins from barley: molecular and functional characterization in housekeeping and defense processes
Autor/es:
  • Martinez Muñoz, Manuel
  • Cambra Marin, Ines
  • Gonzalez-Melendi de Leon, Pablo
  • Santamaria, Maria E.
  • Diaz Rodriguez, Isabel
Tipo de Documento: Ponencia en Congreso o Jornada (Artículo)
Título del Evento: 1st International conference on PLANT PROTEASES
Fechas del Evento: 10/04/2011 - 14/04/2011
Lugar del Evento: Hemava, Suecia
Título del Libro: Proceedings of 1st International conference on PLANT PROTEASES
Fecha: 2011
Materias:
Escuela: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Departamento: Biotecnologia [hasta 2014]
Licencias Creative Commons: Reconocimiento - Sin obra derivada - No comercial

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Resumen

Plant cysteine-proteases (CysProt) represent a well-characterized type of proteolytic enzymes that fulfill tightly regulated physiological functions (senescence and seed germination among others) and defense roles. This article is focused on the group of papain-proteases C1A (family C1, clan CA) and their inhibitors, phytocystatins (PhyCys). In particular, the protease–inhibitor interaction and their mutual participation in specific pathways throughout the plant's life are reviewed. C1A CysProt and PhyCys have been molecularly characterized, and comparative sequence analyses have identified consensus functional motifs. A correlation can be established between the number of identified CysProt and PhyCys in angiosperms. Thus, evolutionary forces may have determined a control role of cystatins on both endogenous and pest-exogenous proteases in these species. Tagging the proteases and inhibitors with fluorescence proteins revealed common patterns of subcellular localization in the endoplasmic reticulum–Golgi network in transiently transformed onion epidermal cells. Further in vivo interactions were demonstrated by bimolecular fluorescent complementation, suggesting their participation in the same physiological processes.

Más información

ID de Registro: 12485
Identificador DC: http://oa.upm.es/12485/
Identificador OAI: oai:oa.upm.es:12485
URL Oficial: http://www.plantproteases.se/
Depositado por: Memoria Investigacion
Depositado el: 08 Ago 2012 11:37
Ultima Modificación: 21 Abr 2016 11:44
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