Identification and Characterization of New Members of Vacuolar H+-Pyrophosphatase Family from Oryza sativa Genome

Identification and Characterization of New Members of Vacuolar H+-Pyrophosphatase Family from... The vacuolar H+-pyrophosphatase (V-PPase) is an electrogenic H+ pump localized in the plant vacuolar membrane. V-PPase from many species has been characterized previously and the corresponding genes/cDNAs have been cloned. Cloning of the V-PPase genes from many plant species has revealed conserved motifs that may correspond to catalytic sites. The completion of the entire DNA sequence of Oryza sativa (430 Mb) presented an opportunity to study the structure and function of V-PPase proteins, and also to identify new members of this family in Oryza sativa. Our analysis identified three novel V-PPase proteins in the Oryza sativa genome that contain functional domains typical of V-PPase. We have designated them as OVP3 to OVP5. The new predicted OVPs have chromosomal locations different from previously characterized V-PPases (OVP1 and OVP2) located on chromosome 6. They all contain three characteristic motifs of V-PPase and also a conserved motif [DE]YYTS, specific to type I V-PPases and involved in coupling PPi hydrolysis to H+ translocation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Identification and Characterization of New Members of Vacuolar H+-Pyrophosphatase Family from Oryza sativa Genome

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Publisher
Nauka/Interperiodica
Copyright
Copyright © 2005 by MAIK "Nauka/Interperiodica"
Subject
Life Sciences; Plant Sciences; Plant Physiology
ISSN
1021-4437
eISSN
1608-3407
D.O.I.
10.1007/s11183-005-0121-7
Publisher site
See Article on Publisher Site

Abstract

The vacuolar H+-pyrophosphatase (V-PPase) is an electrogenic H+ pump localized in the plant vacuolar membrane. V-PPase from many species has been characterized previously and the corresponding genes/cDNAs have been cloned. Cloning of the V-PPase genes from many plant species has revealed conserved motifs that may correspond to catalytic sites. The completion of the entire DNA sequence of Oryza sativa (430 Mb) presented an opportunity to study the structure and function of V-PPase proteins, and also to identify new members of this family in Oryza sativa. Our analysis identified three novel V-PPase proteins in the Oryza sativa genome that contain functional domains typical of V-PPase. We have designated them as OVP3 to OVP5. The new predicted OVPs have chromosomal locations different from previously characterized V-PPases (OVP1 and OVP2) located on chromosome 6. They all contain three characteristic motifs of V-PPase and also a conserved motif [DE]YYTS, specific to type I V-PPases and involved in coupling PPi hydrolysis to H+ translocation.

Journal

Russian Journal of Plant PhysiologySpringer Journals

Published: Nov 15, 2005

References

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