חיפוש מתקדם
Biochemical Society Transactions
Arazi, T., Leeds Inst. for Biotechnology/Agric., School of Biology, University of Leeds, Leeds LS2 9JT, United Kingdom
Kaplan, B., Leeds Inst. for Biotechnology/Agric., School of Biology, University of Leeds, Leeds LS2 9JT, United Kingdom
Sunkar, R., Leeds Inst. for Biotechnology/Agric., School of Biology, University of Leeds, Leeds LS2 9JT, United Kingdom
Fromm, H., Leeds Inst. for Biotechnology/Agric., School of Biology, University of Leeds, Leeds LS2 9JT, United Kingdom
Recently we discovered a tobacco protein (designated NtCBP4) that modulates heavy-metal tolerance in transgenic plants. Structurally, NtCBP4 is similar to mammalian cyclic-nucleotide-gated non-selective cation channels containing six putative transmembrane domains, a predicted pore region, a conserved cyclic-nucleotide-binding domain, and a high-affinity calmodulin-binding site that coincides with its cyclic-nucleotide-binding domain. Transgenic tobacco expressing the plasma-membrane-localized NtCBP4 exhibit improved tolerance to Ni2+ and hypersensitivity to Pb2+, which are associated with a decreased accumulation of Ni2+ and an enhanced accumulation of Pb2+ respectively. Transgenic plants expressing a truncated version of NtCBP4, from which regulatory domains had been removed, have a different phenotype. Here we describe our approach to studying the involvement of NtCBP4 in heavy-metal tolerance and to elucidate its physiological role.
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תנאי שימוש
Cyclic-nucleotide- and Ca2+/calmodulin-regulated channels in plants: Targets for manipulating heavy-metal tolerance, and possible physiological roles
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Arazi, T., Leeds Inst. for Biotechnology/Agric., School of Biology, University of Leeds, Leeds LS2 9JT, United Kingdom
Kaplan, B., Leeds Inst. for Biotechnology/Agric., School of Biology, University of Leeds, Leeds LS2 9JT, United Kingdom
Sunkar, R., Leeds Inst. for Biotechnology/Agric., School of Biology, University of Leeds, Leeds LS2 9JT, United Kingdom
Fromm, H., Leeds Inst. for Biotechnology/Agric., School of Biology, University of Leeds, Leeds LS2 9JT, United Kingdom
Cyclic-nucleotide- and Ca2+/calmodulin-regulated channels in plants: Targets for manipulating heavy-metal tolerance, and possible physiological roles
Recently we discovered a tobacco protein (designated NtCBP4) that modulates heavy-metal tolerance in transgenic plants. Structurally, NtCBP4 is similar to mammalian cyclic-nucleotide-gated non-selective cation channels containing six putative transmembrane domains, a predicted pore region, a conserved cyclic-nucleotide-binding domain, and a high-affinity calmodulin-binding site that coincides with its cyclic-nucleotide-binding domain. Transgenic tobacco expressing the plasma-membrane-localized NtCBP4 exhibit improved tolerance to Ni2+ and hypersensitivity to Pb2+, which are associated with a decreased accumulation of Ni2+ and an enhanced accumulation of Pb2+ respectively. Transgenic plants expressing a truncated version of NtCBP4, from which regulatory domains had been removed, have a different phenotype. Here we describe our approach to studying the involvement of NtCBP4 in heavy-metal tolerance and to elucidate its physiological role.
Scientific Publication
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