| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 280, Issue 13, 12637-12642, April 1, 2005
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Graduate School of Pharmaceutical Sciences, Chiba University, 1-8-1 Inohana, Chuo-ku, Chiba 260-8675, Japan
The properties of the protein encoded by YKL174c (TPO5) were studied. It was found that TPO5 excretes putrescine effectively and spermidine less effectively. 
-Aminobutyric acid slightly inhibited the excretion of putrescine, but basic amino acids did not affect excretion, suggesting that TPO5 preferentially recognizes polyamines. Accordingly, yeast cells transformed with the plasmid encoding YKL174c (TPO5) were resistant to toxicity caused by 120 mM putrescine or by 3 mM spermidine, and a mutant with a disrupted YKL174c (TPO5) gene was sensitive to toxicity by 90 mM putrescine. The growth of this mutant was faster than that of the wild-type strain. In parallel, there was an increase in putrescine and spermidine content of the YKL174c (TPO5) mutant compared with wild-type. It is noted that TPO5 functions as a suppressor of cell growth by excreting polyamines. The level of YKL174c (TPO5) mRNA was increased by the addition of polyamines to the medium. The degree of induction of the mRNA was spermine > spermidine > putrescine. The subcellular localization of TPO5 was determined by immunostaining of hemagglutinin-tagged TPO5, and it was found on Golgi or post-Golgi secretory vesicles. Excretion of putrescine and spermidine by TPO5 was reduced in cells that have mutations in the secretory or endocytic pathways, indicating that both processes are involved in the excretion of polyamines.
Received for publication, September 20, 2004 , and in revised form, January 11, 2005.
* This work was supported by a grant-in-aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology, Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel. 81-43-226-2871; Fax: 81-43-226-2873; E-mail: iga16077{at}p.chiba-u.ac.jp.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  K. Higashi, H. Ishigure, R. Demizu, T. Uemura, K. Nishino, A. Yamaguchi, K. Kashiwagi, and K. Igarashi Identification of a Spermidine Excretion Protein Complex (MdtJI) in Escherichia coli J. Bacteriol., February 1, 2008; 190(3): 872 - 878. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Uemura, K. Kashiwagi, and K. Igarashi Polyamine Uptake by DUR3 and SAM3 in Saccharomyces cerevisiae J. Biol. Chem., March 9, 2007; 282(10): 7733 - 7741. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. N. Tun, C. Santa-Catarina, T. Begum, V. Silveira, W. Handro, E. I. S. Floh, and G. F. E. Scherer Polyamines Induce Rapid Biosynthesis of Nitric Oxide (NO) in Arabidopsis thaliana Seedlings Plant Cell Physiol., March 1, 2006; 47(3): 346 - 354. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Hoshino, E. Momiyama, K. Yoshida, K. Nishimura, S. Sakai, T. Toida, K. Kashiwagi, and K. Igarashi Polyamine Transport by Mammalian Cells and Mitochondria: ROLE OF ANTIZYME AND GLYCOSAMINOGLYCANS J. Biol. Chem., December 30, 2005; 280(52): 42801 - 42808. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Aouida, A. Leduc, R. Poulin, and D. Ramotar AGP2 Encodes the Major Permease for High Affinity Polyamine Import in Saccharomyces cerevisiae J. Biol. Chem., June 24, 2005; 280(25): 24267 - 24276. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
