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 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 Request Permissions
Google Scholar
Right arrow Articles by Morita, T.
Right arrow Articles by Yagi, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Morita, T.
Right arrow Articles by Yagi, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 2004, Vol. 135, No. 2 225-230
© 2004 The Japanese Biochemical Society

MOLECULAR BIOLOGY

Disruption of the plr1 + Gene Encoding Pyridoxal Reductase of Schizosaccharomyces pombe

Tomotake Morita1, Kaoru Takegawa2 and Toshiharu Yagi*,1

1 Department of Bioresources Science, Faculty of Agriculture, Kochi University, Nankoku, Kochi 783-8502; and 2 Department of Life Sciences, Faculty of Agriculture, Kagawa University, Kagawa 761-0795

Pyridoxal (PL) reductase encoded by the plr1+ gene practically catalyzes the irreversible reduction of PL by NADPH to form pyridoxine (PN). The enzyme has been suggested to be involved in the salvage synthesis of pyridoxal 5'-phosphate (PLP), a coenzyme form of vitamin B6, or the excretion of PL as PN from yeast cells. In this study, a PL reductase-disrupted (plr1{Delta}) strain was constructed and its phenotype was examined. The plr1{Delta} cells showed almost the same growth curve as that of wild-type cells in YNB and EMM media. In EMM, the plr1{Delta} strain became flocculent at the late stationary phase for an unknown reason. The plr1{Delta} cells showed low but measurable PL reductase activity catalyzed by some other protein(s) than the enzyme encoded by the plr1+ gene, which maintained the flow of "PL -> PN -> PNP -> PLP" in the salvage synthesis of PLP. The total vitamin B6 and pyridoxamine 5'-phosphate contents in the plr1{Delta} cells were significantly lower than those in the wild-type ones. The percentages of the PLP amount as to the other vitamin B6 compounds were similar in the two cell types. The amount of PL in the culture medium of the disruptant was significantly higher than that in the wild-type. In contrast, PN was much higher in the latter than the former. The plr1{Delta} cells accumulated a 6.1-fold higher amount of PL than the wild-type ones when they were incubated with PL. The results showed that PL reductase encoded by the plr1+ gene is involved in the excretion of PL after reducing it to PN, and may not participate in the salvage pathway for PLP synthesis.

* To whom correspondence should be addressed. Tel/Fax: +81-88-864-5191, E-mail: yagito{at}cc.kochi-u.ac.jp


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
A. Idnurm, F. J. Walton, A. Floyd, J. L. Reedy, and J. Heitman
Identification of ENA1 as a Virulence Gene of the Human Pathogenic Fungus Cryptococcus neoformans through Signature-Tagged Insertional Mutagenesis
Eukaryot. Cell, March 1, 2009; 8(3): 315 - 326.
[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.