Functions of the water soluble chlorophyll-binding protein in plants

Copyright © 2011 Elsevier GmbH. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Journal of plant physiology. - 1979. - 168(2011), 12 vom: 15. Aug., Seite 1444-51
1. Verfasser: Damaraju, Sridevi (VerfasserIn)
Weitere Verfasser: Schlede, Stephanie, Eckhardt, Ulrich, Lokstein, Heiko, Grimm, Bernhard
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2011
Zugriff auf das übergeordnete Werk:Journal of plant physiology
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Light-Harvesting Protein Complexes Peroxides Plant Extracts Plant Proteins Reactive Oxygen Species Xanthophylls Water 059QF0KO0R mehr... Chlorophyll 1406-65-1 Peroxidase EC 1.11.1.7 Oxidoreductases Acting on CH-CH Group Donors EC 1.3.- protochlorophyllide reductase EC 1.3.1.33
Beschreibung
Zusammenfassung:Copyright © 2011 Elsevier GmbH. All rights reserved.
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 accumulation and peroxidase activity at different light intensities, even at high light intensities of 700-900μmol 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
Beschreibung:Date Completed 07.10.2011
Date Revised 30.09.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1618-1328
DOI:10.1016/j.jplph.2011.02.007