scholarly journals High-Light versus Low-Light: Effects on Paired Photosystem II Supercomplex Structural Rearrangement in Pea Plants

2020 ◽  
Vol 21 (22) ◽  
pp. 8643
Author(s):  
Alessandro Grinzato ◽  
Pascal Albanese ◽  
Roberto Marotta ◽  
Paolo Swuec ◽  
Guido Saracco ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Photosystem Ii ◽  
Structural Rearrangement ◽  
Structural Features ◽  
Thylakoid Membranes ◽  
Variable Number ◽  
High Light ◽  
Low Light ◽  
Cryo Electron Microscopy ◽  
Light Effects

In plant grana thylakoid membranes Photosystem II (PSII) associates with a variable number of antenna proteins (LHCII) to form different types of supercomplexes (PSII-LHCII), whose organization is dynamically adjusted in response to light cues, with the C2S2 more abundant in high-light and the C2S2M2 in low-light. Paired PSII-LHCII supercomplexes interacting at their stromal surface from adjacent thylakoid membranes were previously suggested to mediate grana stacking. Here, we present the cryo-electron microscopy maps of paired C2S2 and C2S2M2 supercomplexes isolated from pea plants grown in high-light and low-light, respectively. These maps show a different rotational offset between the two supercomplexes in the pair, responsible for modifying their reciprocal interaction and energetic connectivity. This evidence reveals a different way by which paired PSII-LHCII supercomplexes can mediate grana stacking at diverse irradiances. Electrostatic stromal interactions between LHCII trimers almost completely overlapping in the paired C2S2 can be the main determinant by which PSII-LHCII supercomplexes mediate grana stacking in plants grown in high-light, whereas the mutual interaction of stromal N-terminal loops of two facing Lhcb4 subunits in the paired C2S2M2 can fulfil this task in plants grown in low-light. The high-light induced accumulation of the Lhcb4.3 protein in PSII-LHCII supercomplexes has been previously reported. Our cryo-electron microscopy map at 3.8 Å resolution of the C2S2 supercomplex isolated from plants grown in high-light suggests the presence of the Lhcb4.3 protein revealing peculiar structural features of this high-light-specific antenna important for photoprotection.

Changes in the Stoichiometry of Photosystem II Components as an Adaptive Response to High-Light and Low-Light Conditions during Growth

1986 ◽  
Vol 41 (5-6) ◽  
pp. 597-603 ◽  
Author(s):  
Aloysius Wild ◽  
Matthias Höpfner ◽  
Wolfgang Rühle ◽  
Michael Richter
Keyword(s):  
Photosystem Ii ◽  
Functional Organization ◽  
Photosynthetic Apparatus ◽  
High Light ◽  
Molar Ratio ◽  
Light Conditions ◽  
Low Light ◽  
Pigment System ◽  
Transport Chain ◽  
The One

The effect of different growth light intensities (60 W·m-2, 6 W·m-2) on the performance of the photosynthetic apparatus of mustard plants (Sinapis alba L.) was studied. A distinct decrease in photosystem II content per chlorophyll under low-light conditions compared to high-light conditions was found. For P-680 as well as for Oᴀ and Oв protein the molar ratio between high-light and low-light plants was 1.4 whereas the respective concentrations per chlorophyll showed some variations for P-680 and Oᴀ on the one and Oв protein on the other hand.In addition to the study of photosystem II components, the concentrations of PQ, Cyt f, and P-700 were measured. The light regime during growth had no effect on the amount of P-700 per chlorophyll but there were large differences with respect to PQ and Cyt f. The molar ratio for Cyt f and PQ between high- and low-light leaves was 2.2 and 1.9, respectively.Two models are proposed, showing the functional organization of the pigment system and the electron transport chain in thylakoids of high-light and low-light leaves of mustard plants.

Carotenoids and Photosystem II Characteristics of Upper and Lower Halves of Leaves Acclimated to High Light

1996 ◽  
Vol 23 (6) ◽  
pp. 669 ◽  
Author(s):  
WW Iii Adams ◽  
B Demmig-Adams ◽  
DH Barker ◽  
S Kiley
Keyword(s):  
Chlorophyll Fluorescence ◽  
Photosystem Ii ◽  
Excitation Energy ◽  
Total Energy ◽  
Xanthophyll Cycle ◽  
Lower Surface ◽  
Thylakoid Membranes ◽  
High Light ◽  
Pigment Composition ◽  
Light Gradient

Acclimation of the leaves or stems of four succulent species to different light environments and to the light gradient across high light-acclimated tissues was examined through measurements of chlorophyll fluorescence and characterisation of the pigment composition of the thylakoid membranes. Whereas the total amounts of light striking the upper (sun-exposed) and lower (self-shaded) surfaces were quite different, resulting in a much smaller pool of the xanthophyll cycle carotenoids in the lower halves of high light-acclimated tissues, the conversion state of the xanthophyll cycle (the degree to which violaxanthin is converted to antheraxanthin and zeaxanthin) was similar throughout the tissues during exposure to natural sunlight. Under full sunlight, less than 25% of the light absorbed by the upper surface was utilised through photosynthesis, with the majority of the remaining excitation energy being dissipated thermally. In contrast, a considerably greater fraction of the light absorbed by the lower surface was utilised in photosynthesis, ranging from one-third to more than two-thirds of the total energy absorbed.

scholarly journals Cryo-electron Microscopy Structures of Novel Viruses from Mud Crab Scylla paramamosain with Multiple Infections

2019 ◽  
Vol 93 (7) ◽  
Author(s):  
Yuanzhu Gao ◽  
Shanshan Liu ◽  
Jiamiao Huang ◽  
Qianqian Wang ◽  
Kunpeng Li ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
3D Structure ◽  
Structural Features ◽  
Economic Losses ◽  
Scylla Paramamosain ◽  
Multiple Infections ◽  
Mud Crab ◽  
Cryo Electron Microscopy ◽  
Novel Virus ◽  
Icosahedral Capsid

ABSTRACT Viruses associated with sleeping disease (SD) in crabs cause great economic losses to aquaculture, and no effective measures are available for their prevention. In this study, to help develop novel antiviral strategies, single-particle cryo-electron microscopy was applied to investigate viruses associated with SD. The results not only revealed the structure of mud crab dicistrovirus (MCDV) but also identified a novel mud crab tombus-like virus (MCTV) not previously detected using molecular biology methods. The structure of MCDV at a 3.5-Å resolution reveals three major capsid proteins (VP1 to VP3) organized into a pseudo-T=3 icosahedral capsid, and affirms the existence of VP4. Unusually, MCDV VP3 contains a long C-terminal region and forms a novel protrusion that has not been observed in other dicistrovirus. Our results also reveal that MCDV can release its genome via conformation changes of the protrusions when viral mixtures are heated. The structure of MCTV at a 3.3-Å resolution reveals a T= 3 icosahedral capsid with common features of both tombusviruses and nodaviruses. Furthermore, MCTV has a novel hydrophobic tunnel beneath the 5-fold vertex and 30 dimeric protrusions composed of the P-domains of the capsid protein at the 2-fold axes that are exposed on the virion surface. The structural features of MCTV are consistent with a novel type of virus. IMPORTANCE Pathogen identification is vital for unknown infectious outbreaks, especially for dual or multiple infections. Sleeping disease (SD) in crabs causes great economic losses to aquaculture worldwide. Here we report the discovery and identification of a novel virus in mud crabs with multiple infections that was not previously detected by molecular, immune, or traditional electron microscopy (EM) methods. High-resolution structures of pathogenic viruses are essential for a molecular understanding and developing new disease prevention methods. The three-dimensional (3D) structure of the mud crab tombus-like virus (MCTV) and mud crab dicistrovirus (MCDV) determined in this study could assist the development of antiviral inhibitors. The identification of a novel virus in multiple infections previously missed using other methods demonstrates the usefulness of this strategy for investigating multiple infectious outbreaks, even in humans and other animals.

scholarly journals Cryo-EM reveals unique structural features of the FhuCDB Escherichia coli ferrichrome importer

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Wenxin Hu ◽  
Hongjin Zheng
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Molecular Basis ◽  
Iron Uptake ◽  
Structural Features ◽  
Biological Processes ◽  
Type Ii ◽  
Functional Studies ◽  
Cryo Electron Microscopy ◽  
Translocation Pathway

AbstractAs one of the most elegant biological processes developed in bacteria, the siderophore-mediated iron uptake demands the action of specific ATP-binding cassette (ABC) importers. Although extensive studies have been done on various ABC importers, the molecular basis of these iron-chelated-siderophore importers are still not fully understood. Here, we report the structure of a ferrichrome importer FhuCDB from Escherichia coli at 3.4 Å resolution determined by cryo electron microscopy. The structure revealed a monomeric membrane subunit of FhuB with a substrate translocation pathway in the middle. In the pathway, there were unique arrangements of residues, especially layers of methionines. Important residues found in the structure were interrogated by mutagenesis and functional studies. Surprisingly, the importer’s ATPase activity was decreased upon FhuD binding, which deviated from the current understanding about bacterial ABC importers. In summary, to the best of our knowledge, these studies not only reveal a new structural twist in the type II ABC importer subfamily, but also provide biological insights in the transport of iron-chelated siderophores.

scholarly journals Structures, conformations and distributions of SARS-CoV-2 spike protein trimers on intact virions

2020 ◽  
Author(s):  
Zunlong Ke ◽  
Joaquin Oton ◽  
Kun Qu ◽  
Mirko Cortese ◽  
Vojtech Zila ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Neutralizing Antibodies ◽  
Structural Rearrangement ◽  
Conformational Flexibility ◽  
Target Cells ◽  
Receptor Binding Site ◽  
Cryo Electron Microscopy ◽  
High Resolution Structure ◽  
Virion Surface

AbstractSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude. Heavily glycosylated S trimers bind the ACE2 receptor and mediate entry of virions into target cells. S exhibits extensive conformational flexibility: it modulates the exposure of its receptor binding site and later undergoes complete structural rearrangement to drive fusion of viral and cellular membranes. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy. The structure and distribution of S on the virion surface, however, has not been characterised. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions, determining the high-resolution structure, conformational flexibility and distributions of S trimers in situ on the virion surface. These results provide a basis for understanding the conformations of S present on the virion, and for studying their interactions with neutralizing antibodies.

Cryo-Electron Microscopy of Photosystem II: Towards a High-Resolution Structure

1995 ◽  
pp. 2273-2276 ◽  
Author(s):  
Svetla Stoylova ◽  
Paul McPhie ◽  
Toby D. Flint ◽  
Robert C. Ford ◽  
Andreas Holzenburg
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Photosystem Ii ◽  
Cryo Electron Microscopy ◽  
High Resolution Structure ◽  
Resolution Structure

scholarly journals Multimeric and monomeric photosystem II supercomplexes represent structural adaptations to low- and high-light conditions

2020 ◽  
Vol 295 (43) ◽  
pp. 14537-14545 ◽  
Author(s):  
Eunchul Kim ◽  
Akimasa Watanabe ◽  
Christopher D. P. Duffy ◽  
Alexander V. Ruban ◽  
Jun Minagawa
Keyword(s):  
Photosystem Ii ◽  
Light Harvesting ◽  
Fluorescence Analysis ◽  
Sucrose Density Gradient ◽  
High Light ◽  
Thermal Dissipation ◽  
Structural Basis ◽  
Molecular Architecture ◽  
Structural Adaptation ◽  
Low Light

An intriguing molecular architecture called the “semi-crystalline photosystem II (PSII) array” has been observed in the thylakoid membranes in vascular plants. It is an array of PSII–light-harvesting complex II (LHCII) supercomplexes that only appears in low light, but its functional role has not been clarified. Here, we identified PSII–LHCII supercomplexes in their monomeric and multimeric forms in low light–acclimated spinach leaves and prepared them using sucrose-density gradient ultracentrifugation in the presence of amphipol A8-35. When the leaves were acclimated to high light, only the monomeric forms were present, suggesting that the multimeric forms represent a structural adaptation to low light and that disaggregation of the PSII–LHCII supercomplex represents an adaptation to high light. Single-particle EM revealed that the multimeric PSII–LHCII supercomplexes are composed of two (“megacomplex”) or three (“arraycomplex”) units of PSII–LHCII supercomplexes, which likely constitute a fraction of the semi-crystalline PSII array. Further characterization with fluorescence analysis revealed that multimeric forms have a higher light-harvesting capability but a lower thermal dissipation capability than the monomeric form. These findings suggest that the configurational conversion of PSII–LHCII supercomplexes may serve as a structural basis for acclimation of plants to environmental light.

scholarly journals Structural features of the salivary gland hypertrophy virus of the tsetse fly revealed by cryo-electron microscopy and tomography

Virology ◽  
2018 ◽  
Vol 514 ◽  
pp. 165-169 ◽  
Author(s):  
Igor Orlov ◽  
Robert Drillien ◽  
Danièle Spehner ◽  
Max Bergoin ◽  
Adly M.M. Abd-Alla ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Salivary Gland ◽  
Structural Features ◽  
Tsetse Fly ◽  
Cryo Electron Microscopy ◽  
Salivary Gland Hypertrophy ◽  
Salivary Gland Hypertrophy Virus

scholarly journals A strategy to study intrinsically mixed folded proteins: The structure in solution of ataxin-3

2018 ◽  
Author(s):  
A. Sicorello ◽  
G. Kelly ◽  
A. Oregioni ◽  
J. Nováček ◽  
V. Sklenář ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Nuclear Magnetic Resonance ◽  
Low Complexity ◽  
Structural Features ◽  
Resonance Spectroscopy ◽  
Cryo Electron Microscopy ◽  
Per Se ◽  
Folded Proteins ◽  
First Time ◽  
Structure In Solution

AbstractIt has increasingly become clear over the last two decades that proteins can contain both globular domains and intrinsically unfolded regions which both can contribute to function. While equally interesting, the disordered regions are difficult to study because they usually do not crystallize unless bound to partners and are not easily amenable to cryo-electron microscopy studies. Nuclear magnetic resonance spectroscopy remains the best technique to capture the structural features of intrinsically mixed folded proteins and describe their dynamics. These studies rely on the successful assignment of the spectrum, task not easy per se given the limited spread of the resonances of the disordered residues. Here, we describe assignment of the spectrum of ataxin-3, the protein responsible for the neurodegenerative Machado-Joseph disease. We used a 42 kDa construct containing a globular N-terminal josephin domain and a C-terminal tail which comprises thirteen polyglutamine repeats within a low-complexity region. We developed a strategy which allowed us to achieve 87% assignment of the spectrum. We show that the C-terminal tail is flexible with extended helical regions and interacts only marginally with the rest of the protein. We could also, for the first time, deduce the structure of the polyglutamine repeats within the context of the full-length protein and show that it has a strong helical propensity stabilized by the preceding region.

scholarly journals High-resolution cryo-electron microscopy structure of photosystem II from the mesophilic cyanobacterium, Synechocystis sp. PCC 6803

2021 ◽  
Vol 119 (1) ◽  
pp. e2116765118
Author(s):  
Christopher J. Gisriel ◽  
Jimin Wang ◽  
Jinchan Liu ◽  
David A. Flesher ◽  
Krystle M. Reiss ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Photosystem Ii ◽  
Water Oxidation ◽  
Genetic Manipulation ◽  
Water Channel ◽  
Global Scale ◽  
Cryo Electron Microscopy ◽  
C Terminus ◽  
Pcc 6803

Photosystem II (PSII) enables global-scale, light-driven water oxidation. Genetic manipulation of PSII from the mesophilic cyanobacterium Synechocystis sp. PCC 6803 has provided insights into the mechanism of water oxidation; however, the lack of a high-resolution structure of oxygen-evolving PSII from this organism has limited the interpretation of biophysical data to models based on structures of thermophilic cyanobacterial PSII. Here, we report the cryo-electron microscopy structure of PSII from Synechocystis sp. PCC 6803 at 1.93-Å resolution. A number of differences are observed relative to thermophilic PSII structures, including the following: the extrinsic subunit PsbQ is maintained, the C terminus of the D1 subunit is flexible, some waters near the active site are partially occupied, and differences in the PsbV subunit block the Large (O1) water channel. These features strongly influence the structural picture of PSII, especially as it pertains to the mechanism of water oxidation.

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