scholarly journals A Novel Chloroplast Super-Complex Consisting of the ATP Synthase and Photosystem I Reaction Center

2019 ◽  
Author(s):  
Satarupa Bhaduri ◽  
Sandeep K Singh ◽  
Whitaker Cohn ◽  
S. Saif Hasan ◽  
Julian P. Whitelegge ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Reaction Center ◽  
Atp Synthase ◽  
Photosystem I ◽  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Native Page ◽  
Membrane Protein Complexes ◽  
Reaction Center Complexes

AbstractSeveral ‘super-complexes’ of individual hetero-oligomeric membrane protein complexes, whose function is to facilitate intra-membrane electron and proton transfer and harvesting of light energy, have been previously characterized in the mitochondrial cristae and chloroplast thylakoid membranes. The latter membrane is reported here to also be the location of an intra-membrane super-complex which is dominated by the ATP-synthase and photosystem I (PSI) reaction-center complexes, defined by mass spectrometry, clear-native PAGE and Western Blot analyses. This is the first documented presence of ATP synthase in a super-complex with the PSI reaction-center located in the non-appressed stromal domain of the thylakoid membrane.

scholarly journals Mass spectrometry of intact membrane protein complexes

2013 ◽  
Vol 8 (4) ◽  
pp. 639-651 ◽  
Author(s):  
Arthur Laganowsky ◽  
Eamonn Reading ◽  
Jonathan T S Hopper ◽  
Carol V Robinson
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Protein Complexes ◽  
Intact Membrane ◽  
Membrane Protein Complexes

scholarly journals Controlling release, unfolding and dissociation of membrane protein complexes in the gas phase through collisional cooling

2015 ◽  
Vol 51 (85) ◽  
pp. 15582-15584 ◽  
Author(s):  
Michael Landreh ◽  
Idlir Liko ◽  
Povilas Uzdavinys ◽  
Mathieu Coincon ◽  
Jonathan T. S. Hopper ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Gas Phase ◽  
Protein Complexes ◽  
Intact Membrane ◽  
Collisional Cooling ◽  
Membrane Protein Complexes ◽  
Detergent Micelles

Reduced collisional cooling releases intact membrane protein complexes from detergent micelles for unfolding and dissociation studies by mass spectrometry.

Ion Mobility Mass Spectrometry of Two Tetrameric Membrane Protein Complexes Reveals Compact Structures and Differences in Stability and Packing

2010 ◽  
Vol 132 (44) ◽  
pp. 15468-15470 ◽  
Author(s):  
Sheila C. Wang ◽  
Argyris Politis ◽  
Natalie Di Bartolo ◽  
Vassiliy N. Bavro ◽  
Stephen J. Tucker ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Ion Mobility ◽  
Protein Complexes ◽  
Ion Mobility Mass Spectrometry ◽  
Membrane Protein Complexes

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 Mass spectrometry of membrane protein complexes

2019 ◽  
Vol 400 (7) ◽  
pp. 813-829 ◽  
Author(s):  
Julian Bender ◽  
Carla Schmidt
Keyword(s):  
Mass Spectrometry ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Protein Complexes ◽  
Three Dimensional ◽  
Membrane Protein Complexes ◽  
Hydrophobic Nature ◽  
Alternative Approaches ◽  
Lipid Environment ◽  
And Function

Abstract Membrane proteins are key players in the cell. Due to their hydrophobic nature they require solubilising agents such as detergents or membrane mimetics during purification and, consequently, are challenging targets in structural biology. In addition, their natural lipid environment is crucial for their structure and function further hampering their analysis. Alternative approaches are therefore required when the analysis by conventional techniques proves difficult. In this review, we highlight the broad application of mass spectrometry (MS) for the characterisation of membrane proteins and their interactions with lipids. We show that MS unambiguously identifies the protein and lipid components of membrane protein complexes, unravels their three-dimensional arrangements and further provides clues of protein-lipid interactions.

scholarly journals Top-down mass spectrometry of intact membrane protein complexes reveals oligomeric state and sequence information in a single experiment

2015 ◽  
Vol 24 (8) ◽  
pp. 1292-1300 ◽  
Author(s):  
Albert Konijnenberg ◽  
Ludovic Bannwarth ◽  
Duygu Yilmaz ◽  
Armağan Koçer ◽  
Catherine Venien-Bryan ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Protein Complexes ◽  
Sequence Information ◽  
Oligomeric State ◽  
Top Down ◽  
Single Experiment ◽  
Intact Membrane ◽  
Membrane Protein Complexes ◽  
Top Down Mass Spectrometry

Analysis of Membrane Protein Complexes by Blue Native PAGE

PROTEOMICS ◽  
2006 ◽  
Vol 6 (S2) ◽  
pp. 6-15 ◽  
Author(s):  
Veronika Reisinger ◽  
Lutz Andreas Eichacker
Keyword(s):  
Membrane Protein ◽  
Protein Complexes ◽  
Native Page ◽  
Blue Native Page ◽  
Membrane Protein Complexes ◽  
Blue Native

scholarly journals Dye-ligand chromatographic purification of intact multisubunit membrane protein complexes: application to the chloroplast H+-F0F1-ATP synthase

2000 ◽  
Vol 346 (1) ◽  
pp. 41-44
Author(s):  
Holger SEELERT ◽  
Ansgar POETSCH ◽  
Meino ROHLFS ◽  
Norbert A. DENCHER
Keyword(s):  
Membrane Protein ◽  
Phosphatidic Acid ◽  
Ammonium Sulphate ◽  
Atp Synthase ◽  
Protein Complex ◽  
Protein Complexes ◽  
Atp Synthesis ◽  
Chromatographic Purification ◽  
Membrane Protein Complexes ◽  
Fof1 Atp Synthase

n-Dodecyl-β-D-maltoside was used as a detergent to solubilize the ammonium sulphate precipitate of chloroplast FOF1-ATP synthase, which was purified further by dye-ligand chromatography. Upon reconstitution of the purified protein complex into phosphatidylcholine/phosphatidic acid liposomes, ATP synthesis, driven by an artificial ∆pH/∆ψ, was observed. The highest activity was achieved with ATP synthase solubilized in n-dodecyl-β-D-maltoside followed by chromatography with Red 120 dye. The optimal dye for purification with CHAPS was Green 5. All known subunits were present in the monodisperse proton-translocating ATP synthase preparation obtained from chloroplasts.

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