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Functions of the water soluble chlorophyll-binding protein in plants

  • Functional aspects of water soluble chlorophyll-binding protein (WSCP) in plants were investigated during the courses of leaf senescence, chlorophyll biogenesis, stress response and photoprotection. The cDNA sequence encoding WSCP from cauliflower was cloned into a binary vector to facilitate Agrobacterium tumefaciens mediated transformation of Nicotiana tabacum. The resultant transgenic tobacco plants overexpressed the CauWSCP gene under the control of a 35S-promoter. Analyses of protein and pigment contents indicate that WSCP overexpression does not enhance chlorophyll catabolism in vivo, thus rendering a role of WSCP in Chl degradation unlikely. Accumulation of higher levels of protochlorophyllide in WSCP overexpressor plants corroborates a proposed temporary storage and carrier function of WSCP for chlorophyll and late precursors. Although WSCP overexpressor plants did not show significant differences in non-photochemical quenching of chlorophyll fluorescence, they are characterized by significantly lower zeaxanthin accumulationFunctional aspects of water soluble chlorophyll-binding protein (WSCP) in plants were investigated during the courses of leaf senescence, chlorophyll biogenesis, stress response and photoprotection. The cDNA sequence encoding WSCP from cauliflower was cloned into a binary vector to facilitate Agrobacterium tumefaciens mediated transformation of Nicotiana tabacum. The resultant transgenic tobacco plants overexpressed the CauWSCP gene under the control of a 35S-promoter. Analyses of protein and pigment contents indicate that WSCP overexpression does not enhance chlorophyll catabolism in vivo, thus rendering a role of WSCP in Chl degradation unlikely. Accumulation of higher levels of protochlorophyllide in WSCP overexpressor plants corroborates a proposed temporary storage and carrier function of WSCP for chlorophyll and late precursors. Although WSCP overexpressor plants did not show significant differences in non-photochemical quenching of chlorophyll fluorescence, they are characterized by significantly lower zeaxanthin accumulation and peroxidase activity at different light intensities, even at high light intensities of 700-900 mu mol photons m(-2) s(-1). These results suggest a photoprotective function of the functional chlorophyll binding-WSCP tetramer by shielding of chlorophylls from molecular oxygen.zeige mehrzeige weniger

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Metadaten
Verfasserangaben:Sridevi Damaraju, Stephanie Schlede, Ulrich Eckhardt, Heiko Lokstein, Bernhard Grimm
DOI:https://doi.org/10.1016/j.jplph.2011.02.007
ISSN:0176-1617
Titel des übergeordneten Werks (Englisch):Journal of plant physiology : biochemistry, physiology, molecular biology and biotechnology of plants
Verlag:Elsevier
Verlagsort:Jena
Publikationstyp:Wissenschaftlicher Artikel
Sprache:Englisch
Jahr der Erstveröffentlichung:2011
Erscheinungsjahr:2011
Datum der Freischaltung:26.03.2017
Freies Schlagwort / Tag:Chlorophyll metabolism; Non-photochemical quenching of chlorophyll fluorescence; Photooxidation; Photoprotection; Photosynthesis
Band:168
Ausgabe:12
Seitenanzahl:8
Erste Seite:1444
Letzte Seite:1451
Fördernde Institution:Deutsche Forschungsgemeinschaft [SFB 429, TP A2 [HL] + B9 [BG], GR936 10-1 [BG]]; BMBF
Organisationseinheiten:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer Review:Referiert
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