Molecular speciation and tissue compartmentation of zinc in durum wheat grains with contrasting nutritional status

© 2016 The Authors. New Phytologist © 2016 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 211(2016), 4 vom: 01. Sept., Seite 1255-65
1. Verfasser: Persson, Daniel Pergament (VerfasserIn)
Weitere Verfasser: de Bang, Thomas C, Pedas, Pai R, Kutman, Umit Baris, Cakmak, Ismail, Andersen, Birgit, Finnie, Christine, Schjoerring, Jan K, Husted, Søren
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2016
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't durum wheat endosperm inductively coupled plasma-mass spectrometry (ICP-MS) laser ablation (LA) speciation zinc (Zn) localization zinc (Zn)-binding proteins Plant Proteins mehr... Sulfur 70FD1KFU70 Zinc J41CSQ7QDS Nitrogen N762921K75
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245 1 0 |a Molecular speciation and tissue compartmentation of zinc in durum wheat grains with contrasting nutritional status 
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520 |a Low concentration of zinc (Zn) in the endosperm of cereals is a major factor contributing to Zn deficiency in human populations. We have investigated how combined Zn and nitrogen (N) fertilization affects the speciation and localization of Zn in durum wheat (Triticum durum). Zn-binding proteins were analysed with liquid chromatography ICP-MS and Orbitrap MS(2) , respectively. Laser ablation ICP-MS with simultaneous Zn, sulphur (S) and phosphorus (P) detection was used for bioimaging of Zn and its potential ligands. Increasing the Zn and N supply had a major impact on the Zn concentration in the endosperm, reaching concentrations higher than current breeding targets. The S concentration also increased, but S was only partly co-localized with Zn. The mutual Zn and S enrichment was reflected in substantially more Zn bound to small cysteine-rich proteins (apparent size 10-30 kDa), whereas the response of larger proteins (apparent size > 50 kDa) was only modest. Most of the Zn-responsive proteins were associated with redox- and stress-related processes. This study offers a methodological platform to deepen the understanding of processes behind endosperm Zn enrichment. Novel information is provided on how the localization and speciation of Zn is modified during Zn biofortification of grains 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a durum wheat 
650 4 |a endosperm 
650 4 |a inductively coupled plasma-mass spectrometry (ICP-MS) 
650 4 |a laser ablation (LA) 
650 4 |a speciation 
650 4 |a zinc (Zn) localization 
650 4 |a zinc (Zn)-binding proteins 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Sulfur  |2 NLM 
650 7 |a 70FD1KFU70  |2 NLM 
650 7 |a Zinc  |2 NLM 
650 7 |a J41CSQ7QDS  |2 NLM 
650 7 |a Nitrogen  |2 NLM 
650 7 |a N762921K75  |2 NLM 
700 1 |a de Bang, Thomas C  |e verfasserin  |4 aut 
700 1 |a Pedas, Pai R  |e verfasserin  |4 aut 
700 1 |a Kutman, Umit Baris  |e verfasserin  |4 aut 
700 1 |a Cakmak, Ismail  |e verfasserin  |4 aut 
700 1 |a Andersen, Birgit  |e verfasserin  |4 aut 
700 1 |a Finnie, Christine  |e verfasserin  |4 aut 
700 1 |a Schjoerring, Jan K  |e verfasserin  |4 aut 
700 1 |a Husted, Søren  |e verfasserin  |4 aut 
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