scholarly journals Inter-species variation in the oligomeric states of the higher plant Calvin cycle enzymes glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase

2011 ◽  
Vol 62 (11) ◽  
pp. 3799-3805 ◽  
Author(s):  
Thomas P. Howard ◽  
Julie C. Lloyd ◽  
Christine A. Raines
Nature ◽  
1968 ◽  
Vol 218 (5136) ◽  
pp. 89-90 ◽  
Author(s):  
D. GRAHAM ◽  
A. M. GRIEVE ◽  
ROBERT M. SMILLIE

1998 ◽  
Vol 95 (16) ◽  
pp. 9699-9704 ◽  
Author(s):  
Norbert Wedel ◽  
Jürgen Soll

For higher plant chloroplasts, two key enzymes of the Calvin cycle, phosphoribulokinase (EC 2.7.1.19) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.13), have recently been shown to be oligomerized onto the nonenzymatic peptide CP12. Enzymatic activity depends on complex dissociation, mediated by NADPH. The discovery of genes for CP12 in mosses, green algae, and cyanobacteria, together with the analysis of equivalent multiprotein complexes of Chlamydomonas and Synechocystis suggests that light regulation of Calvin cycle activity via NADPH-mediated reversible phosphoribulokinase/CP12/GAPDH complex dissociation is conserved in all photosynthetic organisms, prokaryotes and eukaryotes. In vitro complex reconstitution assays with heterologously expressed Synechocystis wild-type and mutagenized CP12 demonstrate a conserved subunit composition, stoichiometry, and topology in this complex. Further finding of genes, coding for chimeric proteins, carrying CP12 or parts of it as genetic fusions, indicates that evolution has used the peptide loops of CP12 as universal modules to keep various enzymatic activities under the control of NADP(H). These fusion events occurred at least twice in evolution. First was the fusion of the duplicated genes for CP12 and the ORF4 protein of Anabaena variabilis to the chimeric gene for the heterocyst-specific expressed ORF3 protein, most probably involved in N2 fixation. A second gene fusion, which led to the higher plant chloroplast-specific GAPDH subunit, GAPB, has taken place during the transition from water- to land plants.


1988 ◽  
Vol 151 (1) ◽  
pp. 15-19 ◽  
Author(s):  
D. C. Nelson ◽  
C. A. Williams ◽  
B. A. Farah ◽  
J. M. Shively

2008 ◽  
Vol 55 (2) ◽  
pp. 193-200 ◽  
Author(s):  
E. O. Fedina ◽  
F. G. Karimova ◽  
I. A. Tarchevsky ◽  
I. Yu. Toropygin ◽  
V. A. Khripach

2020 ◽  
Author(s):  
Anja Rödiger ◽  
Birgit Agne ◽  
Dirk Dobritzsch ◽  
Stefan Helm ◽  
Fränze Müller ◽  
...  

AbstractWe report here a detailed analysis of the proteome adjustments that accompany chromoplast differentiation from chloroplasts during bell-pepper fruit ripening. While the two photosystems are disassembled and their constituents degraded, the cytochrome b6f complex, the ATPase complex as well as Calvin cycle enzymes are maintained at high levels up to fully mature chromoplasts. This is also true for ferredoxin (Fd) and Fd-dependent NADP reductase, suggesting that ferredoxin retains a central role in the chromoplasts redox metabolism. There is a significant increase in the amount of enzymes of the typical metabolism of heterotrophic plastids such as the oxidative pentose phosphate pathway (OPPP), amino acid and fatty acid biosynthesis. Enzymes of chlorophyll catabolism and carotenoid biosynthesis increase in abundance, supporting the pigment reorganization that goes together with chromoplast differentiation. The majority of plastid encoded proteins declines but constituents of the plastid ribosome and AccD increase in abundance. Furthermore, the amount of plastid terminal oxidase (PTOX) remains unchanged despite a significant increase in phytoene desaturase (PDS) levels, suggesting that the electrons from phytoene desaturation may be consumed by another oxidase. This may be a particularity of non-climacteric fruits such as bell pepper, that lack a respiratory burst at the onset of fruit ripening.


1996 ◽  
Vol 178 (3) ◽  
pp. 888-893 ◽  
Author(s):  
E R van den Bergh ◽  
S C Baker ◽  
R J Raggers ◽  
P Terpstra ◽  
E C Woudstra ◽  
...  

Polar Biology ◽  
2006 ◽  
Vol 29 (11) ◽  
pp. 909-916 ◽  
Author(s):  
E. Pérez-Torres ◽  
L. Bascuñán ◽  
A. Sierra ◽  
L. A. Bravo ◽  
L. J. Corcuera

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