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The V-ATPase in Paramecium : functional specialization by multiple gene isoforms

The V-ATPase in Paramecium : functional specialization by multiple gene isoforms

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WASSMER, Thomas, Ivonne M. SEHRING, Roland KISSMEHL, Helmut PLATTNER, 2009. The V-ATPase in Paramecium : functional specialization by multiple gene isoforms. In: Pflügers Archiv: European Journal of Physiology. Springer. 457(3), pp. 599-607. ISSN 0365-267X. eISSN 1432-2013. Available under: doi: 10.1007/s00424-007-0417-x

@article{Wassmer2009-01VATPa-58128, title={The V-ATPase in Paramecium : functional specialization by multiple gene isoforms}, year={2009}, doi={10.1007/s00424-007-0417-x}, number={3}, volume={457}, issn={0365-267X}, journal={Pflügers Archiv: European Journal of Physiology}, pages={599--607}, author={Wassmer, Thomas and Sehring, Ivonne M. and Kissmehl, Roland and Plattner, Helmut} }

Plattner, Helmut Sehring, Ivonne M. Wassmer, Thomas 2022-07-22T07:38:13Z Kissmehl, Roland The vacuolar H<sup>+</sup>-ATPase (V-ATPase), a multisubunit, adenosine triphosphate (ATP)-driven proton pump, is essential for numerous cellular processes in all eukaryotes investigated so far. While structure and catalytic mechanism are similar to the evolutionarily related F-type ATPases, the V-ATPase’s main function is to establish an electrochemical proton potential across membranes using ATP hydrolysis. The holoenzyme is formed by two subcomplexes, the transmembraneous V<sub>0</sub> and the cytoplasmic V<sub>1</sub> complexes. Sequencing of the whole genome of the ciliate Paramecium tetraurelia enabled the identification of virtually all the genes encoding V-ATPase subunits in this organism and the studying of the localization of the enzyme and roles in membrane trafficking and osmoregulation. Surprisingly, the number of V-ATPase genes in this free-living protozoan is strikingly higher than in any other species previously studied. Especially abundant are V<sub>0</sub>-a-subunits with as many as 17 encoding genes. This abundance creates the possibility of forming a large number of different V-ATPase holoenzymes by combination and has functional consequences by differential targeting to various organelles. Plattner, Helmut 2022-07-22T07:38:13Z Wassmer, Thomas eng 2009-01 Sehring, Ivonne M. The V-ATPase in Paramecium : functional specialization by multiple gene isoforms Kissmehl, Roland

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