Functional analysis of the C-terminal region of the vacuolar cadmium-transporting rice OsHMA3

• Published in: FEBS letters Vol. 588; no. 5; pp. 789 - 794
• Main Authors: Kumagai, Saori, Suzuki, Tatsuya, Tezuka, Kouichi, Satoh-Nagasawa, Namiko, Takahashi, Hidekazu, Sakurai, Kenji, Watanabe, Akio, Fujimura, Tatsuhito, Akagi, Hiromori
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 03.03.2014
• Subjects: Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - physiology; Amino Acid Substitution; Arabidopsis; Biological Transport; C-terminal domain; Cadmium; Cadmium - metabolism; Cation Transport Proteins - chemistry; Cation Transport Proteins - physiology; Mutagenesis, Site-Directed; Onions; Oryza - enzymology; OsHMA3; P1B-ATPase (HMA); Plant Epidermis - enzymology; Plant Proteins - chemistry; Plant Proteins - physiology; Protein Structure, Tertiary; Protein Transport; Rice; Vacuolar sequestration; Vacuoles - enzymology; P1B-ATPase (HMA); C-terminal domain; Cadmium; OsHMA3; Vacuolar sequestration; Rice; P(1B)-ATPase (HMA)

•The C-terminal domain of OsHMA3 is essential for the transport of Cd in plants.•The first 105aa of the C-terminal region have important roles in OsHMA3 function.•The C-terminal domain is not involved in the subcellular localization of OsHMA3.•The cysteine pair is not necessary for Cd transport in p...