Two Silene vulgaris copper transporters residing in different cellular compartments confer copper hypertolerance by distinct mechanisms when expressed in Arabidopsis thaliana

© 2017 The Authors. New Phytologist © 2017 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 215(2017), 3 vom: 22. Aug., Seite 1102-1114
1. Verfasser: Li, Yanbang (VerfasserIn)
Weitere Verfasser: Iqbal, Mazhar, Zhang, Qianqian, Spelt, Cornelis, Bliek, Mattijs, Hakvoort, Henk W J, Quattrocchio, Francesca M, Koes, Ronald, Schat, Henk
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2017
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Arabidopsis thaliana Silene vulgaris HMA5 P1B-ATPase copper tolerance heavy metal intracellular reallocation Membrane Transport Proteins Plant Proteins mehr... RNA, Messenger Green Fluorescent Proteins 147336-22-9 Copper 789U1901C5
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520 |a Silene vulgaris is a metallophyte of calamine, cupriferous and serpentine soils all over Europe. Its metallicolous populations are hypertolerant to zinc (Zn), cadmium (Cd), copper (Cu) or nickel (Ni), compared with conspecific nonmetallicolous populations. These hypertolerances are metal-specific, but the underlying mechanisms are poorly understood. We investigated the role of HMA5 copper transporters in Cu-hypertolerance of a S. vulgaris copper mine population. Cu-hypertolerance in Silene is correlated and genetically linked with enhanced expression of two HMA5 paralogs, SvHMA5I and SvHMA5II, each of which increases Cu tolerance when expressed in Arabidopsis thaliana. Most Spermatophytes, except Brassicaceae, possess homologs of SvHMA5I and SvHMA5II, which originate from an ancient duplication predating the appearance of spermatophytes. SvHMA5II and the A. thaliana homolog AtHMA5 localize in the endoplasmic reticulum and upon Cu exposure move to the plasma membrane, from where they are internalized and degraded in the vacuole. This resembles trafficking of mammalian homologs and is apparently an extremely ancient mechanism. SvHMA5I, instead, neofunctionalized and always resides on the tonoplast, likely sequestering Cu in the vacuole. Adaption of Silene to a Cu-polluted soil is at least in part due to upregulation of two distinct HMA5 transporters, which contribute to Cu hypertolerance by distinct mechanisms 
650 4 |a Journal Article 
650 4 |a Arabidopsis thaliana 
650 4 |a Silene vulgaris 
650 4 |a HMA5 
650 4 |a P1B-ATPase 
650 4 |a copper tolerance 
650 4 |a heavy metal 
650 4 |a intracellular reallocation 
650 7 |a Membrane Transport Proteins  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a RNA, Messenger  |2 NLM 
650 7 |a Green Fluorescent Proteins  |2 NLM 
650 7 |a 147336-22-9  |2 NLM 
650 7 |a Copper  |2 NLM 
650 7 |a 789U1901C5  |2 NLM 
700 1 |a Iqbal, Mazhar  |e verfasserin  |4 aut 
700 1 |a Zhang, Qianqian  |e verfasserin  |4 aut 
700 1 |a Spelt, Cornelis  |e verfasserin  |4 aut 
700 1 |a Bliek, Mattijs  |e verfasserin  |4 aut 
700 1 |a Hakvoort, Henk W J  |e verfasserin  |4 aut 
700 1 |a Quattrocchio, Francesca M  |e verfasserin  |4 aut 
700 1 |a Koes, Ronald  |e verfasserin  |4 aut 
700 1 |a Schat, Henk  |e verfasserin  |4 aut 
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773 1 8 |g volume:215  |g year:2017  |g number:3  |g day:22  |g month:08  |g pages:1102-1114 
856 4 0 |u http://dx.doi.org/10.1111/nph.14647  |3 Volltext 
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