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

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

Description

Title: Cysteine-proteases and cystatins from barley: molecular and functional characterization in housekeeping and defense processes
Author/s:
  • Martinez Muñoz, Manuel
  • Cambra Marin, Ines
  • Gonzalez-Melendi de Leon, Pablo
  • Santamaria, Maria E.
  • Diaz Rodriguez, Isabel
Item Type: Presentation at Congress or Conference (Article)
Event Title: 1st International conference on PLANT PROTEASES
Event Dates: 10/04/2011 - 14/04/2011
Event Location: Hemava, Suecia
Title of Book: Proceedings of 1st International conference on PLANT PROTEASES
Date: 2011
Subjects:
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

Full text

[img]
Preview
PDF - Requires a PDF viewer, such as GSview, Xpdf or Adobe Acrobat Reader
Download (1MB) | Preview

Abstract

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.

More information

Item ID: 12485
DC Identifier: http://oa.upm.es/12485/
OAI Identifier: oai:oa.upm.es:12485
Official URL: http://www.plantproteases.se/
Deposited by: Memoria Investigacion
Deposited on: 08 Aug 2012 11:37
Last Modified: 21 Apr 2016 11:44
  • Logo InvestigaM (UPM)
  • Logo GEOUP4
  • Logo Open Access
  • Open Access
  • Logo Sherpa/Romeo
    Check whether the anglo-saxon journal in which you have published an article allows you to also publish it under open access.
  • Logo Dulcinea
    Check whether the spanish journal in which you have published an article allows you to also publish it under open access.
  • Logo de Recolecta
  • Logo del Observatorio I+D+i UPM
  • Logo de OpenCourseWare UPM