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Novel type aquaporin SIPs are mainly localized to the ER membrane and show cell‐specific expression in Arabidopsis thaliana
Author(s) -
Ishikawa Fumiyoshi,
Suga Shinobu,
Uemura Tomohiro,
Sato Masa H.,
Maeshima Masayoshi
Publication year - 2005
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/j.febslet.2005.09.076
Subject(s) - aquaporin , arabidopsis , microbiology and biotechnology , arabidopsis thaliana , subcellular localization , cell fractionation , green fluorescent protein , chemistry , function (biology) , biology , biochemistry , membrane , gene , mutant , cytoplasm
We investigated the fourth subgroup of Arabidopsis aquaporin, small and basic intrinsic proteins (SIPs). When they were expressed in yeast, SIP1;1 and SIP1;2, but not SIP2;1, gave water‐channel activity. The transient expression of SIPs linked with green fluorescent protein in Arabidopsis cells and the subcellular fractionation of the tissue homogenate showed their ER localization. The SIP proteins were detected in all of the tissues, except for dry seeds. Histochemical analysis of promoter‐β‐glucuronidase fusions revealed the cell‐specific expression of SIPs. SIP1;1 and SIP1;2 may function as water channels in the ER, while SIP2;1 might act as an ER channel for other small molecules or ions.