Advances in the World of Bacterial Microcompartments

Stewart, Andrew M.; Stewart, Katie L.; Yeates, Todd O.; Bobik, Thomas A.

doi:10.1016/j.tibs.2020.12.002

Cited by 32 publications

(38 citation statements)

References 101 publications

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“…Bacterial microcompartments, or MCPs, are proteinaceous organelle-like structures that are found in nearly 20% of bacteria (Jorda et al, 2013). These supramolecular structures are roughly 100-400 nm in diameter and have evolved to carry out a variety of specialized metabolic functions within the confines of a sequestered environment (Chowdhury et al, 2014;Kerfeld et al, 2010;Axen et al, 2014;Stewart et al, 2021). MCPs are comprised of a variety of signature enzymes encased within a proteinaceous outer shell that prevents the efflux of toxic or volatile intermediates during various multistep enzymatic reactions (Bobik et al, 2015;Kerfeld et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

Structural characterization of hexameric shell proteins from two types of choline-utilization bacterial microcompartments

et al. 2021

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Bacterial microcompartments are large supramolecular structures comprising an outer proteinaceous shell that encapsulates various enzymes in order to optimize metabolic processes. The outer shells of bacterial microcompartments are made of several thousand protein subunits, generally forming hexameric building blocks based on the canonical bacterial microcompartment (BMC) domain. Among the diverse metabolic types of bacterial microcompartments, the structures of those that use glycyl radical enzymes to metabolize choline have not been adequately characterized. Here, six structures of hexameric shell proteins from type I and type II choline-utilization microcompartments are reported. Sequence and structure analysis reveals electrostatic surface properties that are shared between the four types of shell proteins described here.

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Section: Introductionmentioning

confidence: 99%

Structural characterization of hexameric shell proteins from two types of choline-utilization bacterial microcompartments

et al. 2021

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“…Addition of B12 to anaerobically rhamnose grown cells results in further, significantly increased, expression of Pdu proteins, and activation of pdu BMC as evidenced by the production of propionate and 1-propanol (Figure 2), and presence of BMCs detected by TEM [11,19]. It is conceivable, that B12 dependent activation of pdu BMC in anaerobic conditions is not only crucial due to the role of B12 as a cofactor for the signature enzyme PduCDE, a B12-dependent diol dehydratase [20], but also because the PduCDE-B12 complex plays a role in triggering the construction of BMC with the shell proteins thereby encasing pdu enzymes, with the respective signature peptide sequences directing enzyme complexes to the correct locations inside the microcompartment [14, 35-37]. Our results with aerobically and anaerobically rhamnose grown cells, indicate that RNAseq data of pdu operon, including identification of factors involved in control of gene expression, such as regulator PocR, B12-dependent riboswitch(es) and sRNAs [28, 38], require confirmation by proteomics, TEM and metabolic profiling to enable conclusions about activation of functional pdu BMC in L. monocytogenes .…”

Section: Discussionmentioning

confidence: 99%

Impact of vitamin B12 on rhamnose metabolism, stress defense and in-vitro virulence ofListeria monocytogenes

Zeng

Wijnands²,

Boeren

et al. 2021

Preprint

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Listeria monocytogenes is a facultative anaerobe which can cause a severe food-borne infection known as listeriosis. Rhamnose is a deoxyhexose sugar abundant in a range of environments, including the human intestine, and can be degraded by L. monocytogenes in aerobic and anaerobic conditions into lactate, acetate and 1,2-propanediol. Our previous study showed that addition of vitamin B12 stimulates anaerobic growth of L. monocytogenes on rhamnose due to the activation of bacterial microcompartment (BMC)-dependent 1,2-propanediol utilization with concomitant production of propionate and propanol. Notably, anaerobic propanediol metabolism has been linked to virulence of enteric pathogens including Salmonella spp. and L. monocytogenes. In this study we investigate the impact of B12 on aerobic and anerobic growth of L. monocytogenes on rhamnose, and observed growth stimulation and pdu BMC activation only in anaerobically grown cells with B12 added to the medium. Comparative Caco-2 virulence assays, showed that these pdu BMC induced cells have significantly higher translocation efficiency compared to aerobically grown cells (without and with added B12) and non-induced anaerobically grown cells, while adhesion and invasion capacity is similar for all cells. Comparative proteomics analysis showed specific and overlapping responses linked to metabolic shifts, activation of stress defense proteins and virulence factors, with RNA polymerase sigma factor SigL; teichoic acids export ATP-binding protein, TagH; DNA repair and protection proteins RadA and DPS; and glutathione synthase GshAB previously linked to activation of virulence response in L. monocytogenes, uniquely upregulated in anaerobically rhamnose grown pdu BMC induced cells. Our results shed new light into B12 impact on L. monocytogenes competitive fitness and virulence.

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“…Bacterial microcompartments are present in a large number of bacteria. They are known to sequester catabolic pathways that generate a reactive aldehyde intermediate, or encapsulate RuBisCO (ribulose-1,5-bisphosphate carboxylase) and carbonic anhydrase for CO 2 fixation [127,128,165]. The engineering of these compartments has also focused mostly on in vivo applications due to their requirement for in vivo co-assembly of shells and cargo protein.…”

Section: Encapsulation In Proteinaceous Compartments Cages and Virus-like Particlesmentioning

confidence: 99%

Organizing Multi-Enzyme Systems into Programmable Materials for Biocatalysis

Seo

Schmidt‐Dannert

2021

Catalysts

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Significant advances in enzyme discovery, protein and reaction engineering have transformed biocatalysis into a viable technology for the industrial scale manufacturing of chemicals. Multi-enzyme catalysis has emerged as a new frontier for the synthesis of complex chemicals. However, the in vitro operation of multiple enzymes simultaneously in one vessel poses challenges that require new strategies for increasing the operational performance of enzymatic cascade reactions. Chief among those strategies is enzyme co-immobilization. This review will explore how advances in synthetic biology and protein engineering have led to bioinspired co-localization strategies for the scaffolding and compartmentalization of enzymes. Emphasis will be placed on genetically encoded co-localization mechanisms as platforms for future autonomously self-organizing biocatalytic systems. Such genetically programmable systems could be produced by cell factories or emerging cell-free systems. Challenges and opportunities towards self-assembling, multifunctional biocatalytic materials will be discussed.

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Advances in the World of Bacterial Microcompartments

Cited by 32 publications

References 101 publications

Structural characterization of hexameric shell proteins from two types of choline-utilization bacterial microcompartments

Structural characterization of hexameric shell proteins from two types of choline-utilization bacterial microcompartments

Impact of vitamin B12 on rhamnose metabolism, stress defense and in-vitro virulence ofListeria monocytogenes

Organizing Multi-Enzyme Systems into Programmable Materials for Biocatalysis

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