Journal Article

Functional Identification of the Glycerol Transport Activity of <i>Chlamydomonas reinhardtii</i> CrMIP1

Marinela Ioana Anderca, Shinobu Suga, Takuya Furuichi, Kosuke Shimogawara, Masayoshi Maeshima and Shoshi Muto

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 45, issue 9, pages 1313-1319
Published in print September 2004 | ISSN: 0032-0781
Published online September 2004 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pch141
Functional Identification of the Glycerol Transport Activity of Chlamydomonas reinhardtii CrMIP1

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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.

Keywords: Keywords: Aquaporin — Chlamydomonas reinhardtii — Glycerol transport — Heterologous expression — MIP — Sequence analysis.; Abbreviations: CrMIP1, Chlamydomonas reinhardtii MIP1; MIP, major membrane intrinsic protein; NPA motif, asparagine-proline-alanine motif; PIP, plasma membrane intrinsic protein; TIP, tonoplast intrinsic protein; TM, transmembrane domain.

Journal Article.  3912 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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