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Plant Physiol, March 2001, Vol. 125, pp. 1206-1215
Aquaporins Constitute a Large and Highly Divergent Protein Family
in Maize1
François
Chaumont,
François
Barrieu,2
Eva
Wojcik,
Maarten J.
Chrispeels,* and
Rudolf
Jung
Physiological Biochemistry, Université Catholique de Louvain,
B-1348 Louvain-La-Neuve, Belgium (F.C.); Division of Biology,
University of California, San Diego, California 92093-0116 (F.B.,
M.J.C.); and Pioneer Hi-Bred International, Incorporated, 7300 Northwest 62nd Avenue, Johnston, Iowa 50131-1004 (E.W., R.J.)
Aquaporins (AQPs) are an ancient family of channel proteins that
transport water and neutral solutes through a pore and are found in all
eukaryotes and most prokaryotes. A comparison of the amino acid
sequences and phylogenetic analysis of 31 full-length cDNAs of maize
(Zea mays) AQPs shows that they comprise four different groups of highly divergent proteins. We have classified them as plasma
membrane intinsic proteins (PIPs), tonoplast intrinsic proteins,
Nod26-like intrinsic proteins, and small and basic intrinsic proteins.
Amino acid sequence identities vary from 16% to 100%, but all
sequences share structural motifs and conserved amino acids necessary
to stabilize the two loops that form the aqueous pore. Most divergent
are the small and basic integral proteins in which the first of the two
highly conserved Asn-Pro-Ala motifs of the pore is not conserved, but
is represented by alanine-proline-threonine or alanine-proline-serine.
We present a model of ZmPIP1-2 based on the three-dimensional structure
of mammalian AQP1. Tabulation of the number of times that the AQP
sequences are found in a collection of databases that comprises about
470,000 maize cDNAs indicates that a few of the maize AQPs are very
highly expressed and many are not abundantly expressed. The
phylogenetic analysis supports the interpretation that the divergence
of PIPs through gene duplication occurred more recently than the
divergence of the members of the other three subfamilies. This study
opens the way to analyze the function of the proteins in Xenopus
laevis oocytes, determine the tissue specific expression of the
genes, recover insertion mutants, and determine the in planta function.
1
This work was supported by grants from
the Interuniversity "Poles of Attraction" Program of Belgium; the
Prime Minister's Office for Scientific, Technical, and Cultural
Affairs; and the Belgian Fund for Scientific Research (to
F.C.).
2
Present address: Institut de Biologie Vegetale
Moleculaire, Université de Bordeaux I, Avenue des Facultés,
Bât B8, 33405 Talence, France.
*
Corresponding author; e-mail mchrispeels{at}ucsd.edu; fax
858-534-4052.
© 2001 American Society of Plant Physiologists
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