LHPP, the light-harvesting NADPH:protochlorophyllide (Pchlide) oxido¬reductase:Pchlide complex of etiolated plants, is developmentally expressed across the barley leaf gradient

Pollmann, Stephan and Reinbothe, Christiane and Pollmann, Stephan and Desvignes, Claire and Weigele, Martina and Beck, Erwin and Reinbothe, Steffen (2004). LHPP, the light-harvesting NADPH:protochlorophyllide (Pchlide) oxido¬reductase:Pchlide complex of etiolated plants, is developmentally expressed across the barley leaf gradient. "Plant Science", v. 167 (n. 5); pp. 1027-1041. ISSN 0168-9452. https://doi.org/10.1016/j.plantsci.2004.05.044.

Description

Title: LHPP, the light-harvesting NADPH:protochlorophyllide (Pchlide) oxido¬reductase:Pchlide complex of etiolated plants, is developmentally expressed across the barley leaf gradient
Author/s:
  • Pollmann, Stephan
  • Reinbothe, Christiane
  • Pollmann, Stephan
  • Desvignes, Claire
  • Weigele, Martina
  • Beck, Erwin
  • Reinbothe, Steffen
Item Type: Article
Título de Revista/Publicación: Plant Science
Date: 2004
ISSN: 0168-9452
Volume: 167
Subjects:
Freetext Keywords: Chloroplast development; Chlorophyll biosynthesis; Greening; NADPH:protochlorophyllide oxidorediuctases (POR) A and B; Light-harvesting POR:protochlorophyllide complex (LHPP)
Faculty: Centro de Investigación en Biotecnología y Genómica de Plantas (CBGP) (UPM)
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

NADPH:protochlorophyllide oxidoreductase is a key enzyme for the light-induced greening of etiolated angiosperm plants. In barley, two POR proteins exist termed PORA and PORB that have previously been proposed to structurally and functionally cooperate in terms of a higher molecular mass light-harvesting complex named LHPP, in the prolamellar body of etioplasts [Nature 397 (1999) 80]. In this study we examined the expression pattern of LHPP during seedling etiolation and de-etiolation under different experimental conditions. Our results show that LHPP is developmentally expressed across the barley leaf gradient. We further provide evidence that LHPP operates both in plants that etiolate completely before being exposed to white light and in plants that etiolate only partially and begin light-harvesting as soon as traces of light become available in the uppermost parts of the soil. As a result of light absorption, in either case LHPP converts Pchlide a to chlorophyllide (Chlide) a and in turn disintegrates. The released Chlide a, as well as Chlide b produced upon LHPP’s light-dependent dissociation, which leads to the activation of the PORA as a Pchlide b-reducing enzyme, then bind to homologs of water-soluble chlorophyll proteins of Brassicaceae. We propose that these proteins transfer Chlide a and Chlide b to the thylakoids, where their esterification with phytol and assembly into the photosynthetic membrane complexes ultimately takes place. Presumably due to the tight coupling of LHPP synthesis and degradation, as well as WSCP formation and photosynthetic membrane assembly, efficient photo-protection is conferred onto the plant.

More information

Item ID: 14043
DC Identifier: http://oa.upm.es/14043/
OAI Identifier: oai:oa.upm.es:14043
DOI: 10.1016/j.plantsci.2004.05.044
Official URL: http://www.sciencedirect.com/science/article/pii/S0168945204002584
Deposited by: Memoria Investigacion
Deposited on: 20 Dec 2012 17:47
Last Modified: 21 Apr 2016 13:31
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