Functional Identification of the Glycerol Transport Activity of Chlamydomonas reinhardtii CrMIP1 | Zendy

Marinela I. Anderca | Zendy; Shinobu Suga | Zendy; Takuya Furuichi | Zendy; Kosuke Shimogawara | Zendy; Masayoshi Maeshima | Zendy; Shoshi Muto | Zendy

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Functional Identification of the Glycerol Transport Activity of Chlamydomonas reinhardtii CrMIP1

Author(s) -

Marinela I. Anderca,

Shinobu Suga,

Takuya Furuichi,

Kosuke Shimogawara,

Masayoshi Maeshima,

Shoshi Muto

Publication year - 2004

Publication title -

plant and cell physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.975

H-Index - 152

eISSN - 1471-9053

pISSN - 0032-0781

DOI - 10.1093/pcp/pch141

Subject(s) - chlamydomonas reinhardtii , chlamydomonas , biochemistry , saccharomyces cerevisiae , aquaporin , glycerol , yeast , open reading frame , biology , peptide sequence , transit peptide , gene , chemistry , chloroplast , plastid , mutant

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.

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