Journal
PLANT SCIENCE
Volume 181, Issue 1, Pages 23-30Publisher
ELSEVIER IRELAND LTD
DOI: 10.1016/j.plantsci.2011.03.008
Keywords
H+-PPase; Sieves elements-companion cell complex; Phloem; Sucrose; Arabidopsis thaliana
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Funding
- National Research Initiative, USDA National Institute of Food and Agriculture [2007-35100-18382]
- Arizona State University
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Previous literature has shown the presence of a plasma membrane (PM) localized type I H+-PPase in sieve elements of Ricinus communis. Unfortunately, the physiological relevance of these findings remains obscure due to the lack of genetic and molecular reagents to study R. communis. The availability of H+-PPase gain and loss-of-function mutants in Arabidopsis thaliana makes this plant an attractive genetic model to address the question, but data on the PM localization of this H+-PPase in A. thaliana are limited to two proteomic approaches. Here we present the first report on the localization of the type I H+-PPase AVP1 in sieve element-companion cell complexes (SE-CCc) from A. thaliana. Double epifluorescence and immunogold labeling experiments are consistent with the co-localization of AVP1 and PIP1 (a bona fide PM maker) in PM of SE-CCc from A. thaliana. (C) 2011 Elsevier Ireland Ltd. All rights reserved.
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