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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.show moreshow less

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Author details:Sridevi Damaraju, Stephanie Schlede, Ulrich Eckhardt, Heiko Lokstein, Bernhard Grimm
DOI:https://doi.org/10.1016/j.jplph.2011.02.007
ISSN:0176-1617
Title of parent work (English):Journal of plant physiology : biochemistry, physiology, molecular biology and biotechnology of plants
Publisher:Elsevier
Place of publishing:Jena
Publication type:Article
Language:English
Year of first publication:2011
Publication year:2011
Release date:2017/03/26
Tag:Chlorophyll metabolism; Non-photochemical quenching of chlorophyll fluorescence; Photooxidation; Photoprotection; Photosynthesis
Volume:168
Issue:12
Number of pages:8
First page:1444
Last Page:1451
Funding institution:Deutsche Forschungsgemeinschaft [SFB 429, TP A2 [HL] + B9 [BG], GR936 10-1 [BG]]; BMBF
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer review:Referiert
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