Skip Navigation

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (2)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Kobayashi, I.
Right arrow Articles by Tsuzuki, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kobayashi, I.
Right arrow Articles by Tsuzuki, M.
Agricola
Right arrow Articles by Kobayashi, I.
Right arrow Articles by Tsuzuki, M.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 2003, Vol. 44, No. 6 597-606
© 2003 Oxford University Press

Insertional Mutagenesis in a Homologue of a Pi Transporter Gene Confers Arsenate Resistance on Chlamydomonas

Isao Kobayashi1, Shoko Fujiwara1, Kosuke Shimogawara2, Toshikazu Kaise1, Hideaki Usuda2 and Mikio Tsuzuki1,3

1 School of Life Science, Tokyo University of Pharmacy and Life Science, Horinouchi, Hachioji, Tokyo, 192-0392 Japan
2 Laboratory of Chemistry, Teikyo University School of Medicine, Ohtsuka, Hachioji, Tokyo, 192-0395 Japan

An arsenate-resistant mutant AR3 of Chlamydomonas reinhardtii is a recessive mutant generated by random insertional mutagenesis using the ARG7 gene. AR3 shows about 10-fold resistance against arsenate toxicity compared with the wild type. By using a flanking region of an inserted tag as a probe, we cloned the corresponding wild-type allele (PTB1) of a mutated gene, which could completely complement the arsenate-resistance phenotype of AR3. The size of PTB1 cDNA is about 6.0 kb and it encodes a putative protein comprising 1,666 amino acid residues. This protein exhibits significant sequence similarity with the yeast Pho89 protein, which is known to be a Na+/Pi co-transporter, although the PTB1 protein carries an additional Gln- and Gly-rich large hydrophilic region in the middle of its primary structure. Analyses of arsenic accumulation and release revealed that PTB1-disrupted cells show arsenate resistance due to low arsenate uptake. These results suggest that the PTB1 protein is a factor involved in arsenate (or Pi) uptake. Kinetics of Pi uptake revealed that the activity of high-affinity Pi transport component in AR3 is more activated than that in the wild type.

3 Corresponding author: E-mail,mtsu{at}ls.toyaku.ac.jp; Fax, +81-426-76-6721.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Eukaryot CellHome page
J. L. Moseley, C.-W. Chang, and A. R. Grossman
Genome-Based Approaches to Understanding Phosphorus Deprivation Responses and PSR1 Control in Chlamydomonas reinhardtii
Eukaryot. Cell, January 1, 2006; 5(1): 26 - 44.
[Abstract] [Full Text] [PDF]


Home page
Plant Cell PhysiolHome page
I. Kobayashi, S. Fujiwara, K. Shimogawara, C. Sakuma, Y. Shida, T. Kaise, H. Usuda, and M. Tsuzuki
High Intracellular Phosphorus Contents Exhibit a Correlation with Arsenate Resistance in Chlamydomonas Mutants
Plant Cell Physiol., March 1, 2005; 46(3): 489 - 496.
[Abstract] [Full Text] [PDF]



Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.