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Novel type Arabidopsis thaliana H + ‐PPase is localized to the Golgi apparatus
Author(s) -
Mitsuda Nobutaka,
Enami Kazuhiko,
Nakata Mami,
Takeyasu Kunio,
Sato Masa H.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02400-5
Subject(s) - arabidopsis thaliana , golgi apparatus , green fluorescent protein , vacuole , endosome , cytoplasm , arabidopsis , microbiology and biotechnology , biology , subcellular localization , bimolecular fluorescence complementation , brefeldin a , organelle , transport protein , biochemistry , gene , endoplasmic reticulum , mutant , intracellular
Vacuolar H + ‐PPase, a membrane bound proton‐translocating pyrophosphatase found in various species including plants, some protozoan and prokaryotes, has been demonstrated to be localized to the vacuolar membrane in plants. Using a GUS reporter system and a green fluorescent protein (GFP) fusion protein, we investigated the tissue distribution and the subcellular localization, respectively, of a novel type H + ‐PPase encoded by AVP2/AVPL1 identified in the Arabidopsis thaliana genome. We showed that AVP2/AVPL1 is highly expressed at the trichome and the filament of stamen. Furthermore, the fluorescence of GFP‐tagged AVP2/AVPL1 showed small dot‐like structures that were observed throughout the cytoplasm of various Arabidopsis cells under a fluorescent microscope. The distribution of this dot‐like fluorescent pattern was apparently affected by a treatment with brefeldin A. Moreover, we demonstrated that most dot‐like fluorescent structures colocalized with a Golgi resident protein. These findings suggest that this novel type H + ‐PPase resides on the Golgi apparatus rather than the vacuolar membrane.