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Plant and Cell Physiology 2004 45(9):1313-1319; doi:10.1093/pcp/pch141
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© 2004 Oxford University Press

Short Communication

Functional Identification of the Glycerol Transport Activity of Chlamydomonas reinhardtii CrMIP1

Marinela Ioana Anderca1,4, Shinobu Suga1,4, Takuya Furuichi1, Kosuke Shimogawara2, Masayoshi Maeshima1,5 and Shoshi Muto1,3

1 Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601 Japan
2 Laboratory of Chemistry, Teikyo University School of Medicine, Hachioji, Tokyo, 192-0395 Japan
3 Nagoya University Bioscience and Biotechnology Center, Chikusa-ku, Nagoya, 464-8601 Japan

Abstract

By searching a Chlamydomonas expressed sequence tag database and by comparing the retrieved data with homologous sequences from a DNA database, we identified an expressed Chlamydomonas reinhardtii putative major intrinsic protein (MIP) gene. The nucleotide sequence, consisting of 1,631 bp, contains an open reading frame coding for a 300-amino-acid protein named CrMIP1. It possesses conserved NPA motifs, but is not highly homologous to known aquaporins. CrMIP1 was expressed in Saccharomyces cerevisiae and assayed for water and glycerol transport activity. By the stopped-flow spectrophotometric assay, CrMIP1 did not enhance the osmotic water permeability of membrane vesicles of the yeast transformant. However, the transformant cells showed glycerol transport activity in the in vivo assay using [14C]glycerol. This is the first report on the isolation and functional identification of a MIP member from algae.

Footnotes

4 These authors contributed equally to this work.

5 Corresponding author: E-mail, maeshima{at}agr.nagoya-u.ac.jp; Fax, +81-52-789-4096.


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