scholarly journals Lateral heterogeneity of plant thylakoid protein complexes: early reminiscences

2012 ◽  
Vol 367 (1608) ◽  
pp. 3384-3388 ◽  
Author(s):  
Jan M. Anderson
Keyword(s):  
Photosystem Ii ◽  
Thylakoid Membrane ◽  
Random Distribution ◽  
Protein Complexes ◽  
Black Box ◽  
Molecular Organization ◽  
Lateral Heterogeneity ◽  
Light Harvesting Complex ◽  
Thylakoid Protein ◽  
In Series

The concept that the two photosystems of photosynthesis cooperate in series, immortalized in Hill and Bendall's Z scheme, was still a black box that defined neither the structural nor the molecular organization of the thylakoid membrane network into grana and stroma thylakoids. The differentiation of the continuous thylakoid membrane into stacked grana thylakoids interconnected by single stroma thylakoids is a morphological reflection of the non-random distribution of photosystem II/light-harvesting complex of photosystem II, photosystem I and ATP synthase, which became known as lateral heterogeneity.

Vipp1 is required for basic thylakoid membrane formation but not for the assembly of thylakoid protein complexes

2007 ◽  
Vol 45 (2) ◽  
pp. 119-128 ◽  
Author(s):  
Elena Aseeva ◽  
Friederich Ossenbühl ◽  
Claudia Sippel ◽  
Won K. Cho ◽  
Bernhard Stein ◽  
...  
Keyword(s):  
Thylakoid Membrane ◽  
Protein Complexes ◽  
Membrane Formation ◽  
Thylakoid Protein

scholarly journals Structure, Dynamics, and Function in the Major Light-Harvesting Complex of Photosystem II

2012 ◽  
Vol 65 (6) ◽  
pp. 583 ◽  
Author(s):  
Gabriela S. Schlau-Cohen ◽  
Graham R. Fleming
Keyword(s):  
Excited State ◽  
Photosystem Ii ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Electronic Spectroscopy ◽  
Emergent Properties ◽  
Light Harvesting Complex ◽  
Natural Systems ◽  
Harvesting Systems ◽  
And Function

In natural light-harvesting systems, pigment-protein complexes (PPC) convert sunlight to chemical energy with near unity quantum efficiency. PPCs exhibit emergent properties that cannot be simply extrapolated from knowledge of their component parts. In this Perspective, we examine the design principles of PPCs, focussing on the major light-harvesting complex of Photosystem II (LHCII), the most abundant PPC in green plants. Studies using two-dimensional electronic spectroscopy (2DES) provide an incisive tool to probe the electronic, energetic, and spatial landscapes that enable the efficiency observed in photosynthetic light-harvesting. Using the information about energy transfer pathways, quantum effects, and excited state geometry contained within 2D spectra, the excited state properties can be linked back to the molecular structure. This understanding of the structure-function relationships of natural systems constitutes a step towards a blueprint for the construction of artificial light-harvesting devices that can reproduce the efficacy of natural systems.

scholarly journals The unique photosynthetic apparatus of Pinaceae: analysis of photosynthetic complexes in Picea abies

2019 ◽  
Vol 70 (12) ◽  
pp. 3211-3225 ◽  
Author(s):  
Steffen Grebe ◽  
Andrea Trotta ◽  
Azfar A Bajwa ◽  
Marjaana Suorsa ◽  
Peter J Gollan ◽  
...  
Keyword(s):  
Picea Abies ◽  
Boreal Forests ◽  
Protein Complexes ◽  
Photosynthetic Apparatus ◽  
Land Plants ◽  
Two Dimensional ◽  
Protein Database ◽  
Light Harvesting Complex ◽  
Mass Spectrometry Identification ◽  
Thylakoid Protein

Abstract Pinaceae are the predominant photosynthetic species in boreal forests, but so far no detailed description of the protein components of the photosynthetic apparatus of these gymnosperms has been available. In this study we report a detailed characterization of the thylakoid photosynthetic machinery of Norway spruce (Picea abies (L.) Karst). We first customized a spruce thylakoid protein database from translated transcript sequences combined with existing protein sequences derived from gene models, which enabled reliable tandem mass spectrometry identification of P. abies thylakoid proteins from two-dimensional large pore blue-native/SDS-PAGE. This allowed a direct comparison of the two-dimensional protein map of thylakoid protein complexes from P. abies with the model angiosperm Arabidopsis thaliana. Although the subunit composition of P. abies core PSI and PSII complexes is largely similar to that of Arabidopsis, there was a high abundance of a smaller PSI subcomplex, closely resembling the assembly intermediate PSI* complex. In addition, the evolutionary distribution of light-harvesting complex (LHC) family members of Pinaceae was compared in silico with other land plants, revealing that P. abies and other Pinaceae (also Gnetaceae and Welwitschiaceae) have lost LHCB4, but retained LHCB8 (formerly called LHCB4.3). The findings reported here show the composition of the photosynthetic apparatus of P. abies and other Pinaceae members to be unique among land plants.

Optimized native gel systems for separation of thylakoid protein complexes: novel super- and mega-complexes

2011 ◽  
Vol 439 (2) ◽  
pp. 207-214 ◽  
Author(s):  
Sari Järvi ◽  
Marjaana Suorsa ◽  
Virpi Paakkarinen ◽  
Eva-Mari Aro
Keyword(s):  
Membrane Protein ◽  
Thylakoid Membrane ◽  
Protein Complexes ◽  
Higher Plant ◽  
Native Page ◽  
Light Harvesting Complexes ◽  
Thylakoid Protein ◽  
Electrophoresis Method ◽  
Membrane Protein Complexes ◽  
Photosynthetic Machinery

Gel-based analysis of thylakoid membrane protein complexes represents a valuable tool to monitor the dynamics of the photosynthetic machinery. Native-PAGE preserves the components and often also the conformation of the protein complexes, thus enabling the analysis of their subunit composition. Nevertheless, the literature and practical experimentation in the field sometimes raise confusion owing to a great variety of native-PAGE and thylakoid-solubilization systems. In the present paper, we describe optimized methods for separation of higher plant thylakoid membrane protein complexes by native-PAGE addressing particularly: (i) the use of detergent; (ii) the use of solubilization buffer; and (iii) the gel electrophoresis method. Special attention is paid to separation of high-molecular-mass thylakoid membrane super- and mega-complexes from Arabidopsis thaliana leaves. Several novel super- and mega-complexes including PS (photosystem) I, PSII and LHCs (light-harvesting complexes) in various combinations are reported.

Capillary electrophoresis of closely related intrinsic thylakoid membrane proteins of the photosystem II light-harvesting complex (LHC II)

1996 ◽  
Vol 17 (10) ◽  
pp. 1597-1601 ◽  
Author(s):  
Lello Zolla ◽  
Maria Bianchetti ◽  
Anna Maria Timperio ◽  
Giuseppe Scarascia Mugnozza ◽  
Danilo Corradini
Keyword(s):  
Capillary Electrophoresis ◽  
Membrane Proteins ◽  
Photosystem Ii ◽  
Thylakoid Membrane ◽  
Light Harvesting ◽  
Lhc Ii ◽  
Light Harvesting Complex ◽  
Thylakoid Membrane Proteins

The Subcomplex Organization of the Major Chlorophyll a/b-Protein Light- Harvesting Complex of Photosystem II (LHCII) in Barley Thylakoid Membrane

1996 ◽  
Vol 51 (7-8) ◽  
pp. 454-463 ◽  
Author(s):  
Grzegorz Jackowski
Keyword(s):  
Photosystem Ii ◽  
Chlorophyll A ◽  
Isoelectric Focusing ◽  
Molecular Species ◽  
Thylakoid Membrane ◽  
Light Harvesting ◽  
Molecular Forms ◽  
Photosynthetic Membrane ◽  
Light Harvesting Complex

Abstract The major chlorophyll a/b-protein light-harvesting complex of photosystem II (LHCII) isolated form barley photosynthetic membrane was shown to contain five major polypeptides only two of which (26.7 and 25.6 kDa) were found to be its true constituents as judged by the ability to migrate as oligomers in various analytical systems. When analyzed by a vertical-bed non-denaturing isoelectric focusing the LHCII was resolved into five trimeric subcom­plexes (designated 1 -5 in order of decreasing p I) containing either only 26.7 kDa polypeptide (subcomplexes 1 and 2) or 26.7 and 25.6 kDa ones associated at 2:1 ratio (subcomplexes 3 -5) . The polypeptide of 26.7 kDa could be split by denaturing isoelectric focusing into fifteen molecular forms while nine molecular species were found to be constituents of 25.6 kDa polypeptide. The subcomplexes 1 -5 contained molecular forms of one or both polypep­ tides associated in sets of 7 -9 . Our findings favour the view that the apoproteins of LHCII are much more heterogenous than thought before.

The Mechanism of Non-Photochemical Quenching in Plants: Localization and Driving Forces

2020 ◽  
Author(s):  
Alexander V Ruban ◽  
Sam Wilson
Keyword(s):  
Photosystem Ii ◽  
Conformational Change ◽  
Thylakoid Membrane ◽  
Driving Forces ◽  
Higher Plants ◽  
Photochemical Quenching ◽  
Light Harvesting Complex ◽  
Chlorophyll Fluorescence Quenching ◽  
Molecular Events

Abstract Non-photochemical chlorophyll fluorescence quenching (NPQ) remains one of the most studied topics of the 21st century in photosynthesis research. Over the past 30 years, profound knowledge has been obtained on the molecular mechanism of NPQ in higher plants. First, the largely overlooked significance of NPQ in protecting the reaction center of photosystem II (RCII) against damage, and the ways to assess its effectiveness are highlighted. Then, the key in vivo signals that can monitor the life of the major NPQ component, qE, are presented. Finally, recent knowledge on the site of qE and the possible molecular events that transmit ΔpH into the conformational change in the major LHCII [the major trimeric light harvesting complex of photosystem II (PSII)] antenna complex are discussed. Recently, number of reports on Arabidopsis mutants lacking various antenna components of PSII confirmed that the in vivo site of qE rests within the major trimeric LHCII complex. Experiments on biochemistry, spectroscopy, microscopy and molecular modeling suggest an interplay between thylakoid membrane geometry and the dynamics of LHCII, the PsbS (PSII subunit S) protein and thylakoid lipids. The molecular basis for the qE-related conformational change in the thylakoid membrane, including the possible onset of a hydrophobic mismatch between LHCII and lipids, potentiated by PsbS protein, begins to unfold.

Sign in / Sign up

Export Citation Format

Share Document