Towards functional proteomics of membrane protein complexes: analysis of thylakoid membranes from Chlamydomonas reinhardtii

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.

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

10.1101/2019.12.25.888495 ◽

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.

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

PLANT PHYSIOLOGY ◽

10.1104/pp.103.032326 ◽

2004 ◽

Vol 134 (1) ◽

pp. 470-481 ◽

Cited By ~ 120

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

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Conformational Flexibility in Assembly of Photosynthetic Membrane Protein Complexes in vivo

Microscopy and Microanalysis ◽

10.1017/s1431927604881534 ◽

2004 ◽

Vol 10 (S02) ◽

pp. 1496-1497

Author(s):

P A Bullough

Keyword(s):

Membrane Protein ◽

Protein Complexes ◽

Conformational Flexibility ◽

Photosynthetic Membrane ◽

Membrane Protein Complexes

Extended abstract of a paper presented at Microscopy and Microanalysis 2004 in Savannah, Georgia, USA, August 1–5, 2004.

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Three-dimensional crystallization of membrane proteins

Quarterly Reviews of Biophysics ◽

10.1017/s0033583500004625 ◽

1988 ◽

Vol 21 (4) ◽

pp. 429-477 ◽

Cited By ~ 156

Author(s):

W. Kühlbrandt

Keyword(s):

High Resolution ◽

Membrane Proteins ◽

Membrane Protein ◽

Protein Complexes ◽

Three Dimensional ◽

Biological Macromolecules ◽

X Ray ◽

X Ray Crystallography ◽

Membrane Protein Complexes ◽

Essential Prerequisite

As recently as 10 years ago, the prospect of solving the structure of any membrane protein by X-ray crystallography seemed remote. Since then, the threedimensional (3-D) structures of two membrane protein complexes, the bacterial photosynthetic reaction centres of Rhodopseudomonas viridis (Deisenhofer et al. 1984, 1985) and of Rhodobacter sphaeroides (Allen et al. 1986, 1987 a, 6; Chang et al. 1986) have been determined at high resolution. This astonishing progress would not have been possible without the pioneering work of Michel and Garavito who first succeeded in growing 3-D crystals of the membrane proteins bacteriorhodopsin (Michel & Oesterhelt, 1980) and matrix porin (Garavito & Rosenbusch, 1980). X-ray crystallography is still the only routine method for determining the 3-D structures of biological macromolecules at high resolution and well-ordered 3-D crystals of sufficient size are the essential prerequisite.

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