scholarly journals DnaK3 Is Involved in Biogenesis and/or Maintenance of Thylakoid Membrane Protein Complexes in the Cyanobacterium Synechocystis sp. PCC 6803

Life ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 55
Author(s):  
Adrien Thurotte ◽  
Tobias Seidel ◽  
Ruven Jilly ◽  
Uwe Kahmann ◽  
Dirk Schneider
Keyword(s):  
Electron Transfer ◽  
Thylakoid Membrane ◽  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Transfer Reactions ◽  
Ps Ii ◽  
Hsp70 Family ◽  
Membrane Protein Complexes ◽  
Synechocystis Sp ◽  
Pcc 6803

DnaK3, a highly conserved cyanobacterial chaperone of the Hsp70 family, binds to cyanobacterial thylakoid membranes, and an involvement of DnaK3 in the biogenesis of thylakoid membranes has been suggested. As shown here, light triggers synthesis of DnaK3 in the cyanobacterium Synechocystis sp. PCC 6803, which links DnaK3 to the biogenesis of thylakoid membranes and to photosynthetic processes. In a DnaK3 depleted strain, the photosystem content is reduced and the photosystem II activity is impaired, whereas photosystem I is regular active. An impact of DnaK3 on the activity of other thylakoid membrane complexes involved in electron transfer is indicated. In conclusion, DnaK3 is a versatile chaperone required for biogenesis and/or maintenance of thylakoid membrane-localized protein complexes involved in electron transfer reactions. As mentioned above, Hsp70 proteins are involved in photoprotection and repair of PS II in chloroplasts.

scholarly journals Regulatory factors for the assembly of thylakoid membrane protein complexes

2012 ◽  
Vol 367 (1608) ◽  
pp. 3420-3429 ◽  
Author(s):  
Wei Chi ◽  
Jinfang Ma ◽  
Lixin Zhang
Keyword(s):  
Membrane Protein ◽  
Thylakoid Membrane ◽  
Molecular Mechanisms ◽  
Current Knowledge ◽  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Regulatory Factors ◽  
Photosynthetic Organisms ◽  
Photosynthetic Complexes ◽  
Membrane Protein Complexes

Major multi-protein photosynthetic complexes, located in thylakoid membranes, are responsible for the capture of light and its conversion into chemical energy in oxygenic photosynthetic organisms. Although the structures and functions of these photosynthetic complexes have been explored, the molecular mechanisms underlying their assembly remain elusive. In this review, we summarize current knowledge of the regulatory components involved in the assembly of thylakoid membrane protein complexes in photosynthetic organisms. Many of the known regulatory factors are conserved between prokaryotes and eukaryotes, whereas others appear to be newly evolved or to have expanded predominantly in eukaryotes. Their specific features and fundamental differences in cyanobacteria, green algae and land plants are discussed.

scholarly journals Towards Functional Proteomics of Membrane Protein Complexes in Synechocystis sp. PCC 6803

2004 ◽  
Vol 134 (1) ◽  
pp. 470-481 ◽  
Author(s):  
Mirkka Herranen ◽  
Natalia Battchikova ◽  
Pengpeng Zhang ◽  
Alexander Graf ◽  
Sari Sirpiö ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Complexes ◽  
Functional Proteomics ◽  
Membrane Protein Complexes ◽  
Synechocystis Sp ◽  
Pcc 6803

2D-isolation of pure plasma and thylakoid membranes from the cyanobacterium Synechocystis sp. PCC 6803

FEBS Letters ◽  
1998 ◽  
Vol 436 (2) ◽  
pp. 189-192 ◽  
Author(s):  
Birgitta Norling ◽  
Elena Zak ◽  
Bertil Andersson ◽  
Himadri Pakrasi
Keyword(s):  
Thylakoid Membranes ◽  
Synechocystis Sp ◽  
Pcc 6803

scholarly journals The oxygen reduction reaction catalyzed by Synechocystis sp. PCC 6803 flavodiiron proteins

2019 ◽  
Vol 3 (11) ◽  
pp. 3191-3200 ◽  
Author(s):  
Katherine A. Brown ◽  
Zhanjun Guo ◽  
Monika Tokmina-Lukaszewska ◽  
Liam W. Scott ◽  
Carolyn E. Lubner ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Oxygen Reduction Reaction ◽  
Oxygen Reduction ◽  
Reduction Reaction ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Mediated Electron Transfer ◽  
Synechocystis Sp ◽  
Pcc 6803

Photosynthetic flavodiiron proteins catalyze oxygen reduction at non-heme iron sites (brown spheres) using flavin (FMN) mediated electron transfer (black arrows).

Degradation of unassembled and damaged thylakoid proteins

2001 ◽  
Vol 29 (4) ◽  
pp. 427-430 ◽  
Author(s):  
Z. Adam ◽  
O. Ostersetzer
Keyword(s):  
Thylakoid Membrane ◽  
D1 Protein ◽  
Thylakoid Membranes ◽  
Reaction Centre ◽  
Ps Ii ◽  
Plant Genomes ◽  
Thylakoid Membrane Proteins ◽  
Luminal Side ◽  
Cytochrome Complex ◽  
Aaa Protein

To study protein degradation in thylakoid membranes we identified, characterized and cloned thylakoid proteases, and then linked them to known proteolytic processes. Several families of chloroplast proteases were identified and characterized to different extents. FtsH, an ATP-dependent metalloprotease that belongs to the AAA-protein family, was found to be integral to the thylakoid membrane, facing the stroma. It is involved in both the degradation of unassembled subunits of membrane complexes, such as the Rieske Fe-S protein of the cytochrome complex, and the degradation of oxidatively damaged proteins such as the D1 protein of the photosystem II (PS II) reaction centre. Plant genomes contain multiple isomers of this protease but the functional significance of this multiplication is not clear yet. A second protease, the serine ATP-independent DegP, was found to be strongly associated with the luminal side of the thylakoid membrane. Although a specific role has not yet assigned for it, its location suggests that it can degrade luminal soluble proteins as well as luminally exposed regions of thylakoid membrane proteins.

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