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Memorias de investigación
Artículos en revistas:
A cathepsin F-like peptidase involved in barley grain protein mobilization, HvPap-1, is modulated by its own propeptide and by cystatins
Año:2012
Áreas de investigación
  • Ciencias naturales y ciencias de la salud,
  • Biología molecular
Datos
Descripción
Among the C1A cysteine proteases, the plant cathepsin F-like group has been poorly studied. This paper describes the molecular and functional characterization of the HvPap-1 cathepsin F-like protein from barley. This peptidase is N-glycosylated and has to be processed to become active, being its own propeptide an important modulator of the peptidase activity. The expression pattern of its mRNA and protein suggest that it is involved in different proteolytic processes in the barley plant. HvPap-1 peptidase has been purified in E. coli and the recombinant protein is able to degrade different substrates, including barley grain proteins (hordeins, albumins and globulins) stored in the barley endosperm. It has been localised in protein bodies and vesicles of the embryo and it is induced in aleurones by GA treatment. These three features support the HvPap-1 implication in the storage protein mobilization during grain germination. In addition, a complex regulation exerted by the barley cystatins, which are cysteine protease inhibitors and by its own propeptide, is also described
Internacional
Si
JCR del ISI
Si
Título de la revista
Journal of Experimental Botany
ISSN
0022-0957
Factor de impacto JCR
4,818
Información de impacto
Datos JCR del año 2010
Volumen
63
DOI
10.1093/jxb/err313
Número de revista
63
Desde la página
4615
Hasta la página
4629
Mes
SIN MES
Ranking
Esta actividad pertenece a memorias de investigación
Participantes
  • Autor: Ines Cambra Marin (UPM)
  • Autor: Manuel Martinez Muñoz (UPM)
  • Autor: Beatriz Dader (CSIC)
  • Autor: Pablo Gonzalez-Melendi De Leon (UPM)
  • Autor: Jacinto Gandullo (Universidad de Sevilla)
  • Autor: Estrella Santamaria (Universidad de Onatario-Canada)
  • Autor: M. Isabel Diaz Rodriguez (UPM)
Grupos de investigación, Departamentos, Centros e Institutos de I+D+i relacionados
  • Creador: Grupo de Investigación: Interacciones moleculares planta-insecto.
  • Centro o Instituto I+D+i: Centro de Biotecnología y Genómica de Plantas, CBGP
  • Departamento: Biotecnología
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