Comparative analysis of the chloroplast proteomes of a wheat (Triticum aestivum L.) single seed descent line and its parents

Bibliographische Detailangaben
Veröffentlicht in:	Journal of plant physiology. - 1979. - 170(2013), 13 vom: 01. Sept., Seite 1139-47
1. Verfasser:	He, Zhi-Hui (VerfasserIn)
Weitere Verfasser:	Li, Hong-Wei, Shen, Yunkang, Li, Zhen-Sheng, Mi, Hualing
Format:	Online-Aufsatz
Sprache:	English
Veröffentlicht:	2013
Zugriff auf das übergeordnete Werk:	Journal of plant physiology
Schlagworte:	Comparative Study Journal Article Research Support, Non-U.S. Gov't 2-cys Prx 2-cysteine peroxiredoxins ATP synthase ATPase CET Chloroplast Cyclic electron transfer mehr... Cytb(6)f FNR FQR GS MALDI TOF MS/MS NAD(P)H dehydrogenase NDH OEC OEE1 P700 PSI PSII Photosynthesis Proteomics RCA Rubisco TRX m Wheat (Triticum aestivum L.) cyclic electron transfer cytochrome b(6)f ferredoxin-NADP(+) oxidoreductase ferredoxin-plastoquinone reductase glutamine synthase m-type thioredoxin matrix-assisted laser desorption/ionization time of flight oxygen-evolving complex oxygen-evolving enhancer 1 photosystem I photosystem II ribulose-1,5-bisphosphate carboxylase/oxygenase rubisco activase tandem mass spectroscopy the reaction center chlorophylls in PSI Photosystem I Protein Complex Proteome

Beschreibung
Zusammenfassung:	Copyright © 2013 Elsevier GmbH. All rights reserved. To understand the photosynthetic basis in a single seed descent line 10 (SSDL10) of wheat contained high ATP in leaves, the chloroplast proteome was compared to SSDL10 and its parents using a combination of 2-DE and MALDI-TOF MS and MS/MS. More than 300 protein spots could be reproducibly detected in the 2D gel. 18 spots were differentially expressed between SSDL10 and the parents, 16 of which were identified by MS with the localization in chloroplasts. These proteins are grouped into diverse functional categories, including Calvin cycle and electron transport in photosynthesis, redox homeostasis, metabolism, and regulation. In addition to Rubisco large subunit, the content of photosynthetic electron transfers such as chlorophyll a-b binding protein, ATP synthase δ subunit, ferredoxin-NADP⁺ oxidoreductase (FNR) was higher in SSDL10 than in its parents. Furthermore, cyclic electron transfer around photosystem I (CET) was faster in SSDL10 than in the parents. Analysis of NADPH-NBT oxidoreductase activity combined with immuno-detection further revealed that, the activity of two high molecular mass protein complexes containing FNR probably involved, the CET appeared higher in SSDL10 than in the parents. The possible mechanism for the regulative role of CET in photosynthesis in SSDL10 is discussed
Beschreibung:	Date Completed 03.03.2014 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE
ISSN:	1618-1328
DOI:	10.1016/j.jplph.2013.03.016