skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Membrane Targeting of P-type ATPases in Plant Cells

Abstract

How membrane proteins are targeted to specific subcellular locations is a very complex and poorly understood area of research. Our long-term goal is to use P-type ATPases (ion pumps), in a model plant system Arabidopsis, as a paradigm to understand how members of a family of closely related membrane proteins can be targeted to different subcellular locations. The research is divided into two specific aims. The first aim is focused on determining the targeting destination of all 10 ACA-type calcium pumps (Arabidopsis Calcium ATPase) in Arabidopsis. ACAs represent a plant specific-subfamily of plasma membrane-type calcium pumps. In contrast to animals, the plant homologs have been found in multiple membrane systems, including the ER (ACA2), tonoplast (ACA4) and plasma membrane (ACA8). Their high degree of similarity provides a unique opportunity to use a comparative approach to delineate the membrane specific targeting information for each pump. One hypothesis to be tested is that an endomembrane located ACA can be re-directed to the plasma membrane by including targeting information from a plasma membrane isoform, ACA8. Our approach is to engineer domain swaps between pumps and monitor the targeting of chimeric proteins in plant cells using a Green Fluorescence Protein (GFP) as a tag.more » The second aim is to test the hypothesis that heterologous transporters can be engineered into plants and targeted to the plasma membrane by fusing them to a plasma membrane proton pump. As a test case we are evaluating the targeting properties of fusions made between a yeast sodium/proton exchanger (Sod2) and a proton pump (AHA2). This fusion may potentially lead to a new strategy for engineering salt resistant plants. Together these aims are designed to provide fundamental insights into the biogenesis and function of plant cell membrane systems.« less

Authors:
Publication Date:
Research Org.:
The Scripps Research Institute (US)
Sponsoring Org.:
(US)
OSTI Identifier:
831127
DOE Contract Number:  
FG02-03ER15437
Resource Type:
Technical Report
Resource Relation:
Other Information: PBD: 30 Jun 2004
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 72 PHYSICS OF ELEMENTARY PARTICLES AND FIELDS; ANIMALS; ARABIDOPSIS; CALCIUM; ENGINEERS; FLUORESCENCE; HYPOTHESIS; MEMBRANE PROTEINS; MEMBRANES; MONITORS; PLANT CELLS; PLASMA; PROTEINS; PROTONS; YEASTS

Citation Formats

Jeffrey F. Harper, Ph.D. Membrane Targeting of P-type ATPases in Plant Cells. United States: N. p., 2004. Web. doi:10.2172/831127.
Jeffrey F. Harper, Ph.D. Membrane Targeting of P-type ATPases in Plant Cells. United States. doi:10.2172/831127.
Jeffrey F. Harper, Ph.D. Wed . "Membrane Targeting of P-type ATPases in Plant Cells". United States. doi:10.2172/831127. https://www.osti.gov/servlets/purl/831127.
@article{osti_831127,
title = {Membrane Targeting of P-type ATPases in Plant Cells},
author = {Jeffrey F. Harper, Ph.D.},
abstractNote = {How membrane proteins are targeted to specific subcellular locations is a very complex and poorly understood area of research. Our long-term goal is to use P-type ATPases (ion pumps), in a model plant system Arabidopsis, as a paradigm to understand how members of a family of closely related membrane proteins can be targeted to different subcellular locations. The research is divided into two specific aims. The first aim is focused on determining the targeting destination of all 10 ACA-type calcium pumps (Arabidopsis Calcium ATPase) in Arabidopsis. ACAs represent a plant specific-subfamily of plasma membrane-type calcium pumps. In contrast to animals, the plant homologs have been found in multiple membrane systems, including the ER (ACA2), tonoplast (ACA4) and plasma membrane (ACA8). Their high degree of similarity provides a unique opportunity to use a comparative approach to delineate the membrane specific targeting information for each pump. One hypothesis to be tested is that an endomembrane located ACA can be re-directed to the plasma membrane by including targeting information from a plasma membrane isoform, ACA8. Our approach is to engineer domain swaps between pumps and monitor the targeting of chimeric proteins in plant cells using a Green Fluorescence Protein (GFP) as a tag. The second aim is to test the hypothesis that heterologous transporters can be engineered into plants and targeted to the plasma membrane by fusing them to a plasma membrane proton pump. As a test case we are evaluating the targeting properties of fusions made between a yeast sodium/proton exchanger (Sod2) and a proton pump (AHA2). This fusion may potentially lead to a new strategy for engineering salt resistant plants. Together these aims are designed to provide fundamental insights into the biogenesis and function of plant cell membrane systems.},
doi = {10.2172/831127},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Wed Jun 30 00:00:00 EDT 2004},
month = {Wed Jun 30 00:00:00 EDT 2004}
}

Technical Report:

Save / Share: