Self-assembly in the carboxysome: a viral capsid-like protein shell in bacterial cells

2007 ◽  
Vol 35 (3) ◽  
pp. 508-511 ◽  
Author(s):  
T.O. Yeates ◽  
Y. Tsai ◽  
S. Tanaka ◽  
M.R. Sawaya ◽  
C.A. Kerfeld
Keyword(s):  
Self Assembly ◽  
Co2 Fixation ◽  
Closed Shell ◽  
Bacterial Cells ◽  
Protein Assemblies ◽  
Bisphosphate Carboxylase ◽  
Viral Capsids ◽  
Chemoautotrophic Bacteria ◽  
Assembly Principles ◽  
Protein Shell

Many proteins self-assemble to form large supramolecular complexes. Numerous examples of these structures have been characterized, ranging from spherical viruses to tubular protein assemblies. Some new kinds of supramolecular structures are just coming to light, while it is likely there are others that have not yet been discovered. The carboxysome is a subcellular structure that has been known for more than 40 years, but whose structural and functional details are just now emerging. This giant polyhedral body is constructed as a closed shell assembled from several thousand protein subunits. Within this protein shell, the carboxysome encapsulates the CO2-fixing enzymes, Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) and carbonic anhydrase; this arrangement enhances the efficiency of cellular CO2 fixation. The carboxysome is present in many photosynthetic and chemoautotrophic bacteria, and so plays an important role in the global carbon cycle. It also serves as the prototypical member of what appears to be a large class of primitive protein-based organelles in bacteria. A series of crystal structures is beginning to reveal the secrets of how the carboxysome is assembled and how it enhances the efficiency of CO2 fixation. Some of the assembly principles revealed in the carboxysome are reminiscent of those seen in icosahedral viral capsids. In addition, the shell appears to be perforated by pores for metabolite transport into and out of the carboxysome, suggesting comparisons to the pores through oligomeric transmembrane proteins, which serve to transport small molecules across the membrane bilayers of cells and eukaryotic organelles.

scholarly journals Protein interface redesign facilitates the transformation of nanocage building blocks to 1D and 2D nanomaterials

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Xiaorong Zhang ◽  
Yu Liu ◽  
Bowen Zheng ◽  
Jiachen Zang ◽  
Chenyan Lv ◽  
...  
Keyword(s):  
Self Assembly ◽  
Thermotoga Maritima ◽  
Building Blocks ◽  
The Self ◽  
Protein Interface ◽  
Protein Assemblies ◽  
Viral Capsids ◽  
2D Nanomaterials ◽  
External Stimuli ◽  
Artificial Protein

AbstractAlthough various artificial protein nanoarchitectures have been constructed, controlling the transformation between different protein assemblies has largely been unexplored. Here, we describe an approach to realize the self-assembly transformation of dimeric building blocks by adjusting their geometric arrangement. Thermotoga maritima ferritin (TmFtn) naturally occurs as a dimer; twelve of these dimers interact with each other in a head-to-side manner to generate 24-meric hollow protein nanocage in the presence of Ca2+ or PEG. By tuning two contiguous dimeric proteins to interact in a fully or partially side-by-side fashion through protein interface redesign, we can render the self-assembly transformation of such dimeric building blocks from the protein nanocage to filament, nanorod and nanoribbon in response to multiple external stimuli. We show similar dimeric protein building blocks can generate three kinds of protein materials in a manner that highly resembles natural pentamer building blocks from viral capsids that form different protein assemblies.

scholarly journals Virus-Like Particles Produced Using the Brome Mosaic Virus Recombinant Capsid Protein Expressed in a Bacterial System

2021 ◽  
Vol 22 (6) ◽  
pp. 3098
Author(s):  
Aleksander Strugała ◽  
Jakub Jagielski ◽  
Karol Kamel ◽  
Grzegorz Nowaczyk ◽  
Marcin Radom ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Mosaic Virus ◽  
Capsid Protein ◽  
Self Assembly ◽  
Environmental Changes ◽  
Expression System ◽  
Brome Mosaic Virus ◽  
Virus Like Particles ◽  
Assembly Principles ◽  
The Impact

Virus-like particles (VLPs), due to their nanoscale dimensions, presence of interior cavities, self-organization abilities and responsiveness to environmental changes, are of interest in the field of nanotechnology. Nevertheless, comprehensive knowledge of VLP self-assembly principles is incomplete. VLP formation is governed by two types of interactions: protein–cargo and protein–protein. These interactions can be modulated by the physicochemical properties of the surroundings. Here, we used brome mosaic virus (BMV) capsid protein produced in an E. coli expression system to study the impact of ionic strength, pH and encapsulated cargo on the assembly of VLPs and their features. We showed that empty VLP assembly strongly depends on pH whereas ionic strength of the buffer plays secondary but significant role. Comparison of VLPs containing tRNA and polystyrene sulfonic acid (PSS) revealed that the structured tRNA profoundly increases VLPs stability. We also designed and produced mutated BMV capsid proteins that formed VLPs showing altered diameters and stability compared to VLPs composed of unmodified proteins. We also observed that VLPs containing unstructured polyelectrolyte (PSS) adopt compact but not necessarily more stable structures. Thus, our methodology of VLP production allows for obtaining different VLP variants and their adjustment to the incorporated cargo.

scholarly journals Learning RuBisCO's birth and subsequent environmental adaptation

2018 ◽  
Vol 47 (1) ◽  
pp. 179-185 ◽  
Author(s):  
Hiroki Ashida ◽  
Eiichi Mizohata ◽  
Akiho Yokota
Keyword(s):  
Co2 Fixation ◽  
Methanogenic Archaea ◽  
Environmental Adaptation ◽  
Bisphosphate Carboxylase ◽  
The Earth ◽  
Number Of Genes

Abstract It is believed that organisms that first appeared after the formation of the earth lived in a very limited environment, making full use of the limited number of genes. From these early organisms' genes, more were created by replication, mutation, recombination, translocation, and transmission of other organisms' DNA; thus, it became possible for ancient organisms to grow in various environments. The photosynthetic CO2-fixing enzyme RuBisCO (ribulose 1,5-bisphosphate carboxylase/oxygenase) began to function in primitive methanogenic archaea and has been evolved as a central CO2-fixing enzyme in response to the large changes in CO2 and O2 concentrations that occurred in the subsequent 4 billion years. In this review, the processes of its adaptation to be specialized for CO2 fixation will be presented from the viewpoint of functions and structures of RuBisCO.

Enveloped artificial viral capsids self-assembled from anionic β-annulus peptide and cationic lipid bilayer

2020 ◽  
Vol 56 (52) ◽  
pp. 7092-7095
Author(s):  
Hiroto Furukawa ◽  
Hiroshi Inaba ◽  
Fumihito Inoue ◽  
Yoshihiro Sasaki ◽  
Kazunari Akiyoshi ◽  
...  
Keyword(s):  
Lipid Bilayer ◽  
Self Assembly ◽  
Cationic Lipid ◽  
Viral Capsid ◽  
Viral Capsids ◽  
Simple Strategy ◽  
Self Assembled

We demonstrated a simple strategy for constructing enveloped artificial viral capsids by self-assembly of anionic artificial viral capsid and lipid bilayer containing cationic lipid.

scholarly journals Photosynthetic hydrogen production by droplet-based microbial micro-reactors under aerobic conditions

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Zhijun Xu ◽  
Shengliang Wang ◽  
Chunyu Zhao ◽  
Shangsong Li ◽  
Xiaoman Liu ◽  
...  
Keyword(s):  
Hydrogen Production ◽  
Self Assembly ◽  
Spatial Organization ◽  
Oxygen Depletion ◽  
Bacterial Cells ◽  
Multicellular Spheroids ◽  
Two Phase ◽  
Aerobic Conditions ◽  
Micro Reactors ◽  
And Function

AbstractThe spontaneous self-assembly of multicellular ensembles into living materials with synergistic structure and function remains a considerable challenge in biotechnology and synthetic biology. Here, we exploit the aqueous two-phase separation of dextran-in-PEG emulsion micro-droplets for the capture, spatial organization and immobilization of algal cells or algal/bacterial cell communities to produce discrete multicellular spheroids capable of both aerobic (oxygen producing) and hypoxic (hydrogen producing) photosynthesis in daylight under air. We show that localized oxygen depletion results in hydrogen production from the core of the algal microscale reactor, and demonstrate that enhanced levels of hydrogen evolution can be achieved synergistically by spontaneously enclosing the photosynthetic cells within a shell of bacterial cells undergoing aerobic respiration. Our results highlight a promising droplet-based environmentally benign approach to dispersible photosynthetic microbial micro-reactors comprising segregated cellular micro-niches with dual functionality, and provide a step towards photobiological hydrogen production under aerobic conditions.

scholarly journals Geometric description of self-interaction potential in symmetric protein complexes

2019 ◽  
Vol 6 (1) ◽  
Author(s):  
Charly Empereur-Mot ◽  
Hector Garcia-Seisdedos ◽  
Nadav Elad ◽  
Sucharita Dey ◽  
Emmanuel D. Levy
Keyword(s):  
Self Assembly ◽  
Protein Complexes ◽  
Hot Spot ◽  
Point Mutations ◽  
Supramolecular Assembly ◽  
Internal Symmetry ◽  
Crystallographic Structure ◽  
Viral Capsids ◽  
Reliability Estimates ◽  
Order Structures

Abstract Proteins can self-associate with copies of themselves to form symmetric complexes called homomers. Homomers are widespread in all kingdoms of life and allow for unique geometric and functional properties, as reflected in viral capsids or allostery. Once a protein forms a homomer, however, its internal symmetry can compound the effect of point mutations and trigger uncontrolled self-assembly into high-order structures. We identified mutation hot spots for supramolecular assembly, which are predictable by geometry. Here, we present a dataset of descriptors that characterize these hot spot positions both geometrically and chemically, as well as computer scripts allowing the calculation and visualization of these properties for homomers of choice. Since the biological relevance of homomers is not readily available from their X-ray crystallographic structure, we also provide reliability estimates obtained by methods we recently developed. These data have implications in the study of disease-causing mutations, protein evolution and can be exploited in the design of biomaterials.

Self-assembly of a nonanuclear NiII cluster via atmospheric CO2 fixation: synthesis, structure, collision-induced dissociation mass spectrometry and magnetic property

2020 ◽  
Vol 49 (31) ◽  
pp. 10977-10982
Author(s):  
Xue-Fei Tian ◽  
Bao-Qian Ji ◽  
Lei Feng ◽  
Kai Sheng ◽  
Yan-Min Su ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Magnetic Property ◽  
Self Assembly ◽  
Co2 Fixation ◽  
Mixed Ligand ◽  
Atmospheric Co2 ◽  
Collision Induced Dissociation

The atmospheric CO2 was spontaneously fixed into a novel nonanuclear Ni(ii) cluster which has been easily and successfully constructed through a mixed-ligand approach.

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