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Plant Physiol, May 2000, Vol. 123, pp. 111-124
Expression of Water Channel Proteins in Mesembryanthemum
crystallinum1
Hans-Hubert
Kirch,2
Rosario
Vera-Estrella,
Dortje
Golldack,3
Francoise
Quigley,4
Christine B.
Michalowski,
Bronwyn J.
Barkla, and
Hans J.
Bohnert*
Department of Biochemistry, University of Arizona, Biosciences
West, Tucson, Arizona 85721-0088 (H.-H.K., D.G., F.Q., C.B.M.,
H.J.B.); and Departamento de Biología Molecular de Plantas,
Instituto de Biotecnología, University Nacional Autónoma
de México, 510-3 Colonia Miraval, Cuernavaca 62250, México
(R.V.-E., B.J.B.)
We have characterized transcripts for nine major intrinsic proteins
(MIPs), some of which function as water channels (aquaporins), from the
ice plant Mesembryanthemum crystallinum. To determine the cellular distribution and expression of these MIPs,
oligopeptide-based antibodies were generated against MIP-A, MIP-B,
MIP-C, or MIP-F, which, according to sequence and functional
characteristics, are located in the plasma membrane (PM) and tonoplast,
respectively. MIPs were most abundant in cells involved in bulk water
flow and solute flux. The tonoplast MIP-F was found in all cells, while signature cell types identified different PM-MIPs: MIP-A predominantly in phloem-associated cells, MIP-B in xylem parenchyma, and MIP-C in the
epidermis and endodermis of immature roots. Membrane protein analysis
confirmed MIP-F as tonoplast located. MIP-A and MIP-B were found in
tonoplast fractions and also in fractions distinct from either the
tonoplast or PM. MIP-C was most abundant but not exclusive to PM
fractions, where it is expected based on its sequence signature. We
suggest that within the cell, MIPs are mobile, which is similar to
aquaporins cycling through animal endosomes. MIP cycling and the
differential regulation of these proteins observed under conditions of
salt stress may be fundamental for the control of tissue water flux.
1
This work was supported by the U.S. Department
of Agriculture-National Research Initiative (Plant Responses to the
Environment program), by the National Science Foundation International
Program (U.S. and Mexico), by the Arizona Agricultural Experiment
Station, and by private funds. B.J.B. and R.V.-E. were supported by
Consejo Nacional de Ciencia y Tecnológia (no. 25750N) and
Dirección General de Asuntas para el Personal Académico
(no. IN232998). H.-H.K. and D.G. were supported by the Deutsche
Forschungsgemeinschaft (Bonn, Germany).
2
Present address: Institut für Botanik,
Universität Bonn, Bonn, Germany.
3
Present address: Institut für
Pflanzenphysiologie, Universität Bielefeld, Bielefeld, Germany.
4
Present address: Laboratoire de Biologie
Moléculaire des Plantes, Université Grenoble, Grenoble, France.
*
Corresponding author; e-mail bohnerth{at}u.arizona.edu; fax
520-621-1697.
© 2000 American Society of Plant Physiologists
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