TY - JOUR
T1 - Plasma membrane localization of the type I H+-PPase AVP1 in sieve element-companion cell complexes from Arabidopsis thaliana
AU - Paez-Valencia, Julio
AU - Patron-Soberano, Araceli
AU - Rodriguez-Leviz, Alejandra
AU - Sanchez-Lares, Jonathan
AU - Sanchez-Gomez, Concepcion
AU - Valencia-Mayoral, Pedro
AU - Diaz-Rosas, Guadalupe
AU - Gaxiola, Roberto
N1 - Funding Information:
We want to thank Colin Landeros and Paredes Diaz for technical assistance with imaging and EM sample processing, respectively. This work was supported by the National Research Initiative Competitive Grant no. 2007-35100-18382 from the USDA National Institute of Food and Agriculture and Arizona State University start-up funds to R. A. G.
PY - 2011/7
Y1 - 2011/7
N2 - 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.
AB - 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.
KW - Arabidopsis thaliana
KW - H-PPase
KW - Phloem
KW - Sieves elements-companion cell complex
KW - Sucrose
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U2 - 10.1016/j.plantsci.2011.03.008
DO - 10.1016/j.plantsci.2011.03.008
M3 - Article
C2 - 21600394
AN - SCOPUS:79955989571
SN - 0168-9452
VL - 181
SP - 23
EP - 30
JO - Plant Science
JF - Plant Science
IS - 1
ER -