scholarly journals The Assembly of Super-Complexes in the Plant Chloroplast

Biomolecules ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 1839
Author(s):  
Kezhen Qin ◽  
Alisdair R. Fernie ◽  
Youjun Zhang

Increasing evidence has revealed that the enzymes of several biological pathways assemble into larger supramolecular structures called super-complexes. Indeed, those such as association of the mitochondrial respiratory chain complexes play an essential role in respiratory activity and promote metabolic fitness. Dynamically assembled super-complexes are able to alternate between participating in large complexes and existing in a free state. However, the functional significance of the super-complexes is not entirely clear. It has been proposed that the organization of respiratory enzymes into super-complexes could reduce oxidative damage and increase metabolism efficiency. There are several protein complexes that have been revealed in the plant chloroplast, yet little research has been focused on the formation of super-complexes in this organelle. The photosystem I and light-harvesting complex I super-complex’s structure suggests that energy absorbed by light-harvesting complex I could be efficiently transferred to the PSI core by avoiding concentration quenching. Here, we will discuss in detail core complexes of photosystem I and II, the chloroplast ATPase the chloroplast electron transport chain, the Calvin–Benson cycle and a plastid localized purinosome. In addition, we will also describe the methods to identify these complexes.

Author(s):  
Jie Wang ◽  
Long‐Jiang Yu ◽  
Wenda Wang ◽  
Qiujing Yan ◽  
Tingyun Kuang ◽  
...  

1993 ◽  
Vol 340 (1294) ◽  
pp. 381-392 ◽  

Employing discontinuous sucrose density gradient centrifugation of n -dodecyl β-d-maltoside-solubilized thylakoid membranes, three chlorophyll (Chl)-protein complexes containing Chl a , Chl c 2 and peridinin in different proportions, were isolated from the dinoflagellates Symbiodinium microadriaticum, S. kawagutii, S. pilosum and Heterocapsa pygmaea . In S. microadriaticum , the first complex, containing 13% of the total cellular Chl a , and minor quantities of Chl c 2 and peridinin, is associated with polypeptides with apparent molecular mass ( M r ) of 8-9 kDa, and demonstrated inefficient energy transfer from the accessory pigments to Chl a . The second complex contains Chl a , Chl c 2 and peridinin in a molar ratio of 1:1:2, associated with two apoproteins of M r 19-20 kDa, and comprises 45%, 75% and 70%, respectively, of the cellular Chl a , Chl c 2 and peridinin. The efficient energy transfer from Chl c 2 and peridinin to Chl a in this complex is supportive of a light-harvesting function. This Chl a - c 2 - peridin-protein complex represents the major light-harvesting complex in dinoflagellates. The third complex obtained contains 12% of the cellular Chl a , and appears to be the core of photosystem I, associated with a light-harvesting complex. This complex is spectroscopically similar to analogous preparations from different taxonomic groups, but demonstrates a unique apoprotein composition. Antibodies against the water-soluble peridinin-Chl a -protein (sPCP) light-harvesting complexes failed to cross-react with any of the thylakoid-associated complexes, as did antibodies against Chl a - c -fucoxanthin apoprotein (from diatoms). Antibodies against the P 700 apoprotein of plants did not cross-react with the photosystem I complex. Similar results were observed in the other dinoflagellates.


Biochemistry ◽  
2001 ◽  
Vol 40 (4) ◽  
pp. 1029-1036 ◽  
Author(s):  
Egbert J. Boekema ◽  
Poul Erik Jensen ◽  
Eberhard Schlodder ◽  
Jan F. L. van Breemen ◽  
Henny van Roon ◽  
...  

Biochemistry ◽  
2006 ◽  
Vol 45 (22) ◽  
pp. 6947-6955 ◽  
Author(s):  
Enrico Engelmann ◽  
Giuseppe Zucchelli ◽  
Anna Paola Casazza ◽  
Doriano Brogioli ◽  
Flavio M. Garlaschi ◽  
...  

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