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.…
Verfasserangaben: | Sridevi Damaraju, Stephanie Schlede, Ulrich Eckhardt, Heiko Lokstein, Bernhard Grimm |
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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 |