PMID: 11607406Jun 15, 1993Paper

Calvin cycle multienzyme complexes are bound to chloroplast thylakoid membranes of higher plants in situ

Proceedings of the National Academy of Sciences of the United States of America
K H SüssK Adler

Abstract

Further evidence is provided that the Calvin cycle enzymes ribose-5-phosphate isomerase (EC 5.3.1.6), ribulose-5-phosphate kinase (Ru-5-P-K, EC 2.7.1.19), ribulose-1,5-bisphosphate carboxylase (RuP2Case, EC 4.1.1.39), glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12), sedoheptulose-1,7-bisphosphatase (Sed-1,7-bPase, EC 3.1.3.37), and electron transport protein ferredoxin-NADP+ reductase (FNR, EC 1.18.1.1) are organized into stable CO2-fixing multienzyme complexes with a molecular mass of 900 kDa. Limited trypsinolysis combined with immunoblotting revealed that all of chloroplast stromal Ru-5-P-K and GAPDH is located in enzyme complexes. The Calvin cycle enzyme complexes remain intact indefinitely at lower ionic strength but dissociate into components at KCl concentrations >250 mM. Immunoelectron microscopy showed that Ru-5-P-K, GAPDH, Sed-1,7-bPase, and FNR are bound to stroma-faced thylakoid membranes in situ, whereas RuP2Case and RuP2Case activase are randomly distributed throughout chloroplasts. The results indicate that membrane-bound enzyme supercomplexes may play an important role in photosynthesis.

References

Jul 1, 1991·The Plant Cell·G SaalbachK Müntz
Jan 1, 1987·Annual Review of Biochemistry·P A Srere
Apr 15, 1988·European Journal of Biochemistry·B GonteroJ Ricard
Sep 30, 1986·Biochemical and Biophysical Research Communications·J K Sainis, G C Harris
Nov 5, 1988·Journal of Molecular Biology·J JaninC Chothia
Oct 1, 1966·Proceedings of the National Academy of Sciences of the United States of America·R G Jensen, J A Bassham
Dec 1, 1988·Plant Physiology·S P RobinsonA R Portis

❮ Previous
Next ❯

Citations

Feb 27, 1999·Comptes rendus de l'Académie des sciences. Série III, Sciences de la vie·P BaretF Cadet
Sep 16, 2003·Journal of Structural Biology·James B AndersonLouise E Anderson
Mar 7, 2008·Proceedings of the National Academy of Sciences of the United States of America·Thomas P HowardChristine A Raines
Feb 1, 2011·Antioxidants & Redox Signaling·Marika LindahlThomas Kieselbach
Feb 24, 2005·Annual Review of Plant Biology·Brenda S J Winkel
Mar 23, 2011·PloS One·Stephan KruegerDirk Steinhauser
Sep 18, 1997·Proceedings of the National Academy of Sciences of the United States of America·N WedelB K Paap
Mar 5, 2014·Journal of Experimental Botany·Chloe SingletonNicholas Smirnoff
Sep 14, 2006·Photosynthesis Research·Sofía AndaluzAnunciación Abadía
Aug 30, 2008·Current Opinion in Biotechnology·Robert J ConradoMatthew P DeLisa
Sep 15, 2005·The New Phytologist·Lee J Sweetlove, Alisdair R Fernie
Apr 22, 2005·Biochimica Et Biophysica Acta·Diksha Narhar Dani, Jayashree Krishna Sainis
Apr 11, 2003·Journal of Plant Physiology·Jayashree Krishna SainisGautam Kumar Dey
Jun 16, 2011·Biotechnology Advances·Y-H Percival Zhang
Apr 7, 2000·The Journal of Biological Chemistry·M K Geck, F C Hartman
Jul 18, 2020·Frontiers in Plant Science·Janithri S WickramanayakeFiona L Goggin
Sep 19, 2003·The Journal of Biological Chemistry·Keisuke HamadaMasashi Miyano
May 6, 2020·Antioxidants & Redox Signaling·Youjun Zhang, Alisdair R Fernie
Dec 7, 2007·The Plant Cell·James Uniacke, William Zerges
May 1, 2021·Nanoscale·Tyler D JorgensonRené M Overney
Oct 6, 1998·Protein Expression and Purification·R P DunfordT A Dyer

❮ Previous
Next ❯

Related Feeds

Biosynthetic Transformations

Biosyntheic transformtions are multi-step, enzyme-catalyzed processes where substrates are converted into more complex products in living organisms. Simple compounds are modified, converted into other compounds, or joined together to form macromolecules. Discover the latest research on biosynthetic transformations here.