Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell

Sutter, Markus; Greber, B.J.; Aussignargues, Clément; Kerfeld, Cheryl A.

doi:10.1126/science.aan3289

Cited by 198 publications

(378 citation statements)

References 34 publications

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“…Other proteinaceous organelles, such as bacterial microcompartments, are comprised of many different protein subunits and thus entail a higher degree of complexity. Although significant progress has been made towards understanding the molecular principles governing these complex systems 1,10 , our incomplete understanding is still a bottleneck for repurposing such systems as synthetic organelles.…”

Section: Discussionmentioning

confidence: 99%

“…The ability to incorporate similar functional properties in engineered organisms could lead to significant improvements in metabolic engineering and recombinant protein expression 5,6 . However, efforts to reprogram naturally-occurring compartments for synthetic applications are challenging due to their inherent complexity and the large number of different biomacromolecules involved [7][8][9][10] . We therefore identified the encapsulin family of self-assembling prokaryotic proteins as a highly engineerable candidate suitable for designing programmable synthetic organelles in eukaryotes within their interior as part of the self-assembly process to tailor the activity of packaged components.…”

Section: Introductionmentioning

confidence: 99%

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Prokaryotic nanocompartments form synthetic organelles in a eukaryote

Lau

Giessen

Altenburg

et al. 2018

Preprint

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Compartmentalization of proteins into organelles is a promising strategy for enhancing the productivity of engineered eukaryotic organisms. However, approaches that co-opt endogenous organelles may be limited by the potential for unwanted crosstalk and disruption of native metabolic functions. Here, we present the construction of synthetic non-endogenous organelles in the eukaryotic yeast Saccharomyces cerevisiae, based on the prokaryotic family of self-assembling proteins known as encapsulins. We establish that encapsulins self-assemble to form nanoscale compartments in yeast, and that heterologous proteins can be selectively targeted for compartmentalization. Housing destabilized proteins within encapsulin compartments affords protection against proteolytic degradation in vivo, while the interaction between split protein components is enhanced upon co-localization within the compartment interior. Furthermore, encapsulin compartments can support enzymatic catalysis, with substrate turnover observed for an encapsulated yeast enzyme. Encapsulin compartments therefore represent a modular platform, orthogonal to existing organelles, for programming synthetic compartmentalization in eukaryotes.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Prokaryotic nanocompartments form synthetic organelles in a eukaryote

Lau

Giessen

Altenburg

et al. 2018

Preprint

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“…Recognition of the homology among BMC shell proteins using bioinformatics has led to the identification of a multitude of functionally diverse BMCs, found across 19 out of the 29 established bacterial phyla and also in several candidate phyla (Figure 2A) 6 . Moreover, new methods of visualization such as atomic force microscopy 19 , the crystal structure determination of an intact BMC shell 20 and labeling BMCs with fluorescent proteins 21–23 have provided new insights into BMC structure, assembly and subcellular localization. This knowledge has enabled the engineering of BMCs for new applications in synthetic biology 24–26 .…”

Section: Introductionmentioning

confidence: 99%

Bacterial microcompartments

et al. 2018

Self Cite

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Bacterial microcompartments (BMCs) are self-assembling organelles that consist of an enzymatic core that is encapsulated by a selectively permeable protein shell. The potential to form BMCs is widespread, found across the Kingdom Bacteria. BMCs have crucial roles in carbon dioxide fixation in autotrophs and the catabolism of organic substrates in heterotrophs. They contribute to the metabolic versatility of bacteria, providing a competitive advantage in specific environmental niches. Although BMCs were first visualized more than sixty years ago, it is mainly in the last decade that progress has been made in understanding their metabolic diversity and the structural basis of their assembly and function. This progress has not only heightened our understanding of their role in microbial metabolism but it is also beginning to enable their use in a variety of applications in synthetic biology. In this Review, we focus on recent insights into the structure, assembly, diversity and function of BMCs.

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“…The geometric assembly of proteins leads, for example, to the formation of molecular nanomachines and hyperstructures such as the ATP synthase complex and the cytoskeletal microtubules respectively (Alfaro‐Aco and Petry, 2015; Ruhle and Leister, 2015). Proteins can also self‐assemble in planar geometric configurations to make the S‐layer lattices of some bacteria and archaea (Sleytr et al ., 2014) and into distinctive 3D geometries such as bacterial intracellular microcompartments and viral capsids (Uetrecht et al ., 2011; Sutter et al ., 2017). These natural designs have inspired the synthesis of novel nanomaterials and protocols for protein functionalization and controlled association that modulate the material's properties and enable new functions (Yang et al ., 2016).…”

Section: Introductionmentioning

confidence: 99%

Harnessing the power of microbial nanowires

Reguera

2018

Microbial Biotechnology

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SummaryThe reduction of iron oxide minerals and uranium in model metal reducers in the genus Geobacter is mediated by conductive pili composed primarily of a structurally divergent pilin peptide that is otherwise recognized, processed and assembled in the inner membrane by a conserved Type IVa pilus apparatus. Electronic coupling among the peptides is promoted upon assembly, allowing the discharge of respiratory electrons at rates that greatly exceed the rates of cellular respiration. Harnessing the unique properties of these conductive appendages and their peptide building blocks in metal bioremediation will require understanding of how the pilins assemble to form a protein nanowire with specialized sites for metal immobilization. Also important are insights into how cells assemble the pili to make an electroactive matrix and grow on electrodes as biofilms that harvest electrical currents from the oxidation of waste organic substrates. Genetic engineering shows promise to modulate the properties of the peptide building blocks, protein nanowires and current‐harvesting biofilms for various applications. This minireview discusses what is known about the pilus material properties and reactions they catalyse and how this information can be harnessed in nanotechnology, bioremediation and bioenergy applications.

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Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell

Cited by 198 publications

References 34 publications

Prokaryotic nanocompartments form synthetic organelles in a eukaryote

Prokaryotic nanocompartments form synthetic organelles in a eukaryote

Bacterial microcompartments

Harnessing the power of microbial nanowires

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