| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J Biol Chem, Vol. 275, Issue 2, 1294-1299, January 14, 2000
From the Institute of Plant Physiology, Altenbergrain 21, 3013 Bern, Switzerland and the ¶ Institute of Plant Genetics and
Crop Plant Research, Corrensstrasse 3, 06466 Gatersleben, Germany
Plant cells contain a complete oxidative
pentose phosphate pathway in the chloroplasts, but an incomplete
pathway was proposed to be present in the cytosol, with cytosolic (cyt)
isoforms of ribulose-5-phosphate 3-epimerase (RPEase) and other
non-oxidative branch enzymes being undetectable. Here we present for
the first time the identification, cloning, and properties of a
cyt-RPEase in rice (Oryza sativa) and presence of its
homologues in other plant species. Recombinant cyt-RPEase is a
homodimer of 24.3-kDa subunits such as in the case of the animal and
yeast enzymes, whereas the chloroplast (chl) RPEase is a hexamer.
Cytosolic and chloroplastic RPEases cannot be separated by anion
exchange chromatography. Since plant cyt-RPEase is more closely related
in its primary structure to homologous enzymes in animal and yeast
cells than to the chloroplast RPEase, the plant nuclear genes coding
for cytosolic and chloroplast RPEases were most likely derived from eubacteria and cyanobacteria, respectively. Accumulation of
cyt-RPEase-mRNA and protein is high in root cells, lacking
chl-RPEase, and lower in green tissue. These and other observations
support the view that green and non-green plant cells possess a
complete oxidative pentose phosphate pathway in the cytosol.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF189365.
Identification, Cloning, and Properties of Cytosolic
D-Ribulose-5-phosphate 3-Epimerase from Higher Plants*
,
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The 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. Current address:
Institut für Forstbotanik und Baumphysiologie, Am Flughafen 17, 79085 Freiburg i. Br., Germany. Tel.: 49-761-2038303; Fax: 49-761-2038302; E-mail: kopriva@uni-freiburg.de.
§
Present address: Institut für Forstbotanik und
Baumphysiologie, Am Flughafen 17, 79085 Freiburg i. Br., Germany.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  D. Hutchings, S. Rawsthorne, and M. J. Emes Fatty acid synthesis and the oxidative pentose phosphate pathway in developing embryos of oilseed rape (Brassica napus L.) J. Exp. Bot., February 1, 2005; 56(412): 577 - 585. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Marmagne, M.-A. Rouet, M. Ferro, N. Rolland, C. Alcon, J. Joyard, J. Garin, H. Barbier-Brygoo, and G. Ephritikhine Identification of New Intrinsic Proteins in Arabidopsis Plasma Membrane Proteome Mol. Cell. Proteomics, July 1, 2004; 3(7): 675 - 691. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Eicks, V. Maurino, S. Knappe, U.-I. Flugge, and K. Fischer The Plastidic Pentose Phosphate Translocator Represents a Link between the Cytosolic and the Plastidic Pentose Phosphate Pathways in Plants Plant Physiology, February 1, 2002; 128(2): 512 - 522. [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 |
