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

Wassmer, Thomas; Sehring, Ivonne M.; Kissmehl, Roland; Plattner, Helmut

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

Dateien

Zu diesem Dokument gibt es keine Dateien.

Datum

2009

Autor:innen

Wassmer, Thomas

Sehring, Ivonne M.

Kissmehl, Roland

Plattner, Helmut

DOI (zitierfähiger Link)

https://doi.org/10.1007/s00424-007-0417-x

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Pflügers Archiv: European Journal of Physiology. Springer. 2009, 457(3), pp. 599-607. ISSN 0365-267X. eISSN 1432-2013. Available under: doi: 10.1007/s00424-007-0417-x

Zusammenfassung

The vacuolar H⁺-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 V₀ and the cytoplasmic V₁ 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 V₀-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.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

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. 2009, 457(3), pp. 599-607. ISSN 0365-267X. eISSN 1432-2013. Available under: doi: 10.1007/s00424-007-0417-x

BibTex

@article{Wassmer2009-01VATPa-58128,
  year={2009},
  doi={10.1007/s00424-007-0417-x},
  title={The V-ATPase in Paramecium : functional specialization by multiple gene isoforms},
  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}
}

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    <dcterms:abstract xml:lang="eng">The vacuolar H&lt;sup&gt;+&lt;/sup&gt;-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&lt;sub&gt;0&lt;/sub&gt; and the cytoplasmic V&lt;sub&gt;1&lt;/sub&gt; 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&lt;sub&gt;0&lt;/sub&gt;-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.</dcterms:abstract>
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