A native Zn/Cd pumping P(1B) ATPase from natural overexpression in a hyperaccumulator plant

We report here the first purification of a P(1B) type ATPase, a group of transporters that occurs in bacteria, plants and animals incl. humans, from a eukaryotic organism in native state. TcHMA4 is a P(1B) type ATPase that is highly expressed in the Cd/Zn hyperaccumulator plant Thlaspi caerulescens...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2007-11, Vol.363 (1), p.51-56
Main Authors: Parameswaran, Aravind, Leitenmaier, Barbara, Yang, Mingjie, Kroneck, Peter M H, Welte, Wolfram, Lutz, Gabriela, Papoyan, Ashot, Kochian, Leon V, Küpper, Hendrik
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - chemistry
Cadmium - chemistry
Enzyme Activation
Plant Extracts - chemistry
Plant Proteins - chemistry
Proton Pumps - chemistry
Substrate Specificity
Thlaspi - enzymology
Up-Regulation
Zinc - chemistry
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Summary:We report here the first purification of a P(1B) type ATPase, a group of transporters that occurs in bacteria, plants and animals incl. humans, from a eukaryotic organism in native state. TcHMA4 is a P(1B) type ATPase that is highly expressed in the Cd/Zn hyperaccumulator plant Thlaspi caerulescens and contains a C-terminal 9-histidine repeat. After isolation from roots, we purified TcHMA4 protein via metal affinity chromatography. The purified protein exhibited Cd- and Zn-activated ATPase activity after reconstitution into lipid vesicles, showing that it was in its native state. Gels of crude root extract and of the purified protein revealed TcHMA4-specific bands of about 50 and 60kDa, respectively, while the TcHMA4 mRNA predicts a single protein with a size of 128kDa. This indicates the occurrence of post-translational processing; the properties of the two bands were characterised by their activity and binding properties.
ISSN:0006-291X