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2.
Nat Commun ; 14(1): 6061, 2023 09 28.
Article in English | MEDLINE | ID: mdl-37770429

ABSTRACT

Many bacterial species use Type VI secretion systems (T6SSs) to deliver anti-bacterial effector proteins into neighbouring bacterial cells, representing an important mechanism of inter-bacterial competition. Specific immunity proteins protect bacteria from the toxic action of their own effectors, whilst orphan immunity proteins without a cognate effector may provide protection against incoming effectors from non-self competitors. T6SS-dependent Rhs effectors contain a variable C-terminal toxin domain (CT), with the cognate immunity protein encoded immediately downstream of the effector. Here, we demonstrate that Rhs1 effectors from two strains of Serratia marcescens, the model strain Db10 and clinical isolate SJC1036, possess distinct CTs which both display NAD(P)+ glycohydrolase activity but belong to different subgroups of NADase from each other and other T6SS-associated NADases. Comparative structural analysis identifies conserved functions required for NADase activity and reveals that unrelated NADase immunity proteins utilise a common mechanism of effector inhibition. By replicating a natural recombination event, we show successful functional exchange of CTs and demonstrate that Db10 encodes an orphan immunity protein which provides protection against T6SS-delivered SJC1036 NADase. Our findings highlight the flexible use of Rhs effectors and orphan immunity proteins during inter-strain competition and the repeated adoption of NADase toxins as weapons against bacterial cells.


Subject(s)
Serratia , Type VI Secretion Systems , Serratia/genetics , NAD+ Nucleosidase/genetics , NAD+ Nucleosidase/metabolism , Bacterial Proteins/metabolism , Type VI Secretion Systems/genetics , Type VI Secretion Systems/metabolism , Serratia marcescens/metabolism
3.
Mol Microbiol ; 119(3): 326-339, 2023 03.
Article in English | MEDLINE | ID: mdl-36627840

ABSTRACT

The bacterial Type VI secretion system (T6SS) is a dynamic macromolecular structure that promotes inter- and intra-species competition through the delivery of toxic effector proteins into neighbouring cells. The T6SS contains 14 well-characterised core proteins necessary for effector delivery (TssA-M, PAAR). In this study, we have identified a novel accessory component required for optimal T6SS activity in the opportunistic pathogen Serratia marcescens, which we name TagV. Deletion of tagV, which encodes an outer membrane lipoprotein, caused a reduction in the T6SS-dependent antibacterial activity of S. marcescens Db10. Mutants of S. marcescens lacking the core component TssJ, a distinct outer membrane lipoprotein previously considered essential for T6SS firing, retained a modest T6SS activity that could be abolished through deletion of tagV. TagV did not interact with the T6SS membrane complex proteins TssL or TssM, but is proposed to bind to peptidoglycan, indicating that the mechanism by which TagV promotes T6SS firing differs from that of TssJ. Homologues of tagV were identified in several other bacterial genera, suggesting that the accessory function of TagV is not restricted to S. marcescens. Together, our findings support the existence of a second, TssJ-independent mechanism for T6SS firing that is dependent upon the activity of TagV proteins.


Subject(s)
Type VI Secretion Systems , Type VI Secretion Systems/genetics , Type VI Secretion Systems/metabolism , Bacterial Proteins/genetics , Bacterial Proteins/metabolism , Serratia marcescens/genetics , Membrane Proteins/metabolism
4.
Acta Crystallogr F Struct Biol Commun ; 79(Pt 1): 8-16, 2023 Jan 01.
Article in English | MEDLINE | ID: mdl-36598351

ABSTRACT

Bacteria exploit specialized secretion systems to assist in competition for resources, in collaboration and in communication. Here, a protocol for the recombinant production, purification and crystallization of a protein linked to the Acinetobacter baumannii type VI secretion system is provided. A high-resolution structure of this trimeric protein is reported, revealing the characteristic dual ß-α-ß subunit fold typical of longer subunit members of the tautomerase superfamily. The protein does not appear to be toxic to bacteria or yeast under the conditions tested. The possible biological role of this protein is discussed.


Subject(s)
Acinetobacter baumannii , Type VI Secretion Systems , Type VI Secretion Systems/genetics , Acinetobacter baumannii/genetics , Crystallography, X-Ray , Bacterial Secretion Systems , Bacteria
5.
Nat Commun ; 13(1): 5195, 2022 09 03.
Article in English | MEDLINE | ID: mdl-36057639

ABSTRACT

The genus Serratia has been studied for over a century and includes clinically-important and diverse environmental members. Despite this, there is a paucity of genomic information across the genus and a robust whole genome-based phylogenetic framework is lacking. Here, we have assembled and analysed a representative set of 664 genomes from across the genus, including 215 historic isolates originally used in defining the genus. Phylogenomic analysis of the genus reveals a clearly-defined population structure which displays deep divisions and aligns with ecological niche, as well as striking congruence between historical biochemical phenotyping data and contemporary genomics data. We highlight the genomic, phenotypic and plasmid diversity of Serratia, and provide evidence of different patterns of gene flow across the genus. Our work provides a framework for understanding the emergence of clinical and other lineages of Serratia.


Subject(s)
Genome, Bacterial , Genomics , Genome, Bacterial/genetics , Phylogeny , Plasmids , Serratia/genetics
6.
FEMS Microbiol Rev ; 45(6)2021 11 23.
Article in English | MEDLINE | ID: mdl-34156081

ABSTRACT

Bacteria inhabit all known ecological niches and establish interactions with organisms from all kingdoms of life. These interactions are mediated by a wide variety of mechanisms and very often involve the secretion of diverse molecules from the bacterial cells. The Type VI secretion system (T6SS) is a bacterial protein secretion system that uses a bacteriophage-like machinery to secrete a diverse array of effectors, usually translocating them directly into neighbouring cells. These effectors display toxic activity in the recipient cell, making the T6SS an effective weapon during inter-bacterial competition and interactions with eukaryotic cells. Over the last two decades, microbiology research has experienced a shift towards using systems-based approaches to study the interactions between diverse organisms and their communities in an ecological context. Here, we focus on this aspect of the T6SS. We consider how our perspective of the T6SS has developed and examine what is currently known about the impact that bacteria deploying the T6SS can have in diverse environments, including niches associated with plants, insects and mammals. We consider how T6SS-mediated interactions can affect host organisms by shaping their microbiota, as well as the diverse interactions that can be established between different microorganisms through the deployment of this versatile secretion system.


Subject(s)
Type VI Secretion Systems , Animals , Bacteria , Bacterial Proteins , Bacterial Secretion Systems , Microbial Interactions
7.
Microbiology (Reading) ; 166(9): 854-860, 2020 09.
Article in English | MEDLINE | ID: mdl-32731905

ABSTRACT

Maturation of [NiFe]-hydrogenases often involves specific proteases responsible for cleavage of the catalytic subunits. Escherichia coli HycI is the protease dedicated to maturation of the Hydrogenase-3 isoenzyme, a component of formate hydrogenlyase-1. In this work, it is demonstrated that a Pectobacterium atrosepticum HycI homologue, HyfK, is required for hydrogenase-4 activity, a component of formate hydrogenlyase-2, in that bacterium. The P. atrosepticum ΔhyfK mutant phenotype could be rescued by either P. atrosepticum hyfK or E. coli hycI on a plasmid. Conversely, an E. coli ΔhycI mutant was complemented by either E. coli hycI or P. atrosepticum hyfK in trans. E. coli is a rare example of a bacterium containing both hydrogenase-3 and hydrogenase-4, however the operon encoding hydrogenase-4 has no maturation protease gene. This work suggests HycI should be sufficient for maturation of both E. coli formate hydrogenlyases, however no formate hydrogenlyase-2 activity was detected in any E. coli strains tested here.


Subject(s)
Escherichia coli/enzymology , Hydrogenase/metabolism , Pectobacterium/enzymology , Peptide Hydrolases/metabolism , Catalytic Domain , Enzyme Activation , Escherichia coli/genetics , Hydrogen/metabolism , Isoenzymes/metabolism , Operon , Pectobacterium/genetics , Peptide Hydrolases/genetics
8.
Cell Microbiol ; 22(9): e13241, 2020 09.
Article in English | MEDLINE | ID: mdl-32592518

ABSTRACT

The Type VI secretion system (T6SS) is a protein translocation nanomachine widespread among Gram-negative bacteria and used as a means to deliver effectors directly into target bacterial or eukaryotic cells. These effectors have a wide variety of functions within target cells that ultimately help the secreting cell gain a competitive fitness advantage. Here, we discuss the different ways in which these effectors can be delivered by the T6SS and the diverse mechanisms by which they exert their noxious action upon recipient cells. We also highlight the existence of roles for T6SS effectors beyond simply the killing of neighbouring cells.


Subject(s)
Bacteria/metabolism , Bacterial Proteins/metabolism , Gram-Negative Bacteria/metabolism , Type VI Secretion Systems/metabolism , Bacteria/genetics , Bacterial Proteins/genetics , Protein Transport , Type VI Secretion Systems/genetics
9.
Nat Commun ; 10(1): 5484, 2019 12 02.
Article in English | MEDLINE | ID: mdl-31792213

ABSTRACT

Type VI secretion systems (T6SSs) are nanomachines widely used by bacteria to deliver toxic effector proteins directly into neighbouring cells. However, the modes of action of many effectors remain unknown. Here we report that Ssp6, an anti-bacterial effector delivered by a T6SS of the opportunistic pathogen Serratia marcescens, is a toxin that forms ion-selective pores. Ssp6 inhibits bacterial growth by causing depolarisation of the inner membrane in intoxicated cells, together with increased outer membrane permeability. Reconstruction of Ssp6 activity in vitro demonstrates that it forms cation-selective pores. A survey of bacterial genomes reveals that genes encoding Ssp6-like effectors are widespread in Enterobacteriaceae and often linked with T6SS genes. We conclude that Ssp6 and similar proteins represent a new family of T6SS-delivered anti-bacterial effectors.


Subject(s)
Bacterial Proteins/metabolism , Cations/metabolism , Serratia marcescens/metabolism , Type VI Secretion Systems/metabolism , Anti-Bacterial Agents/metabolism , Anti-Bacterial Agents/toxicity , Bacterial Proteins/genetics , Bacterial Proteins/toxicity , Cell Membrane/drug effects , Cell Membrane/genetics , Cell Membrane/metabolism , Escherichia coli/drug effects , Escherichia coli/genetics , Escherichia coli/growth & development , Escherichia coli/metabolism , Gene Expression Regulation, Bacterial , Genome, Bacterial , Protein Transport , Serratia marcescens/genetics , Type VI Secretion Systems/genetics , Type VI Secretion Systems/toxicity
10.
Mol Microbiol ; 112(5): 1440-1452, 2019 11.
Article in English | MEDLINE | ID: mdl-31420965

ABSTRACT

Pectobacterium atrosepticum SCRI1043 is a phytopathogenic Gram-negative enterobacterium. Genomic analysis has identified that genes required for both respiration and fermentation are expressed under anaerobic conditions. One set of anaerobically expressed genes is predicted to encode an important but poorly understood membrane-bound enzyme termed formate hydrogenlyase-2 (FHL-2), which has fascinating evolutionary links to the mitochondrial NADH dehydrogenase (Complex I). In this work, molecular genetic and biochemical approaches were taken to establish that FHL-2 is fully functional in P. atrosepticum and is the major source of molecular hydrogen gas generated by this bacterium. The FHL-2 complex was shown to comprise a rare example of an active [NiFe]-hydrogenase-4 (Hyd-4) isoenzyme, itself linked to an unusual selenium-free formate dehydrogenase in the final complex. In addition, further genetic dissection of the genes encoding the predicted membrane arm of FHL-2 established surprisingly that the majority of genes encoding this domain are not required for physiological hydrogen production activity. Overall, this study presents P. atrosepticum as a new model bacterial system for understanding anaerobic formate and hydrogen metabolism in general, and FHL-2 function and structure in particular.


Subject(s)
Formate Dehydrogenases/metabolism , Formates/metabolism , Hydrogen/metabolism , Hydrogenase/metabolism , Multienzyme Complexes/metabolism , Pectobacterium/metabolism , Anaerobiosis/physiology , Formate Dehydrogenases/genetics , Hydrogenase/genetics , Multienzyme Complexes/genetics , NADH Dehydrogenase/metabolism , Oxidation-Reduction , Pectobacterium/enzymology , Pectobacterium/genetics , Plants/microbiology
11.
J Fungi (Basel) ; 5(2)2019 Jun 14.
Article in English | MEDLINE | ID: mdl-31197124

ABSTRACT

Microbes typically exist in mixed communities and display complex synergistic and antagonistic interactions. The Type VI secretion system (T6SS) is widespread in Gram-negative bacteria and represents a contractile nano-machine that can fire effector proteins directly into neighbouring cells. The primary role assigned to the T6SS is to function as a potent weapon during inter-bacterial competition, delivering antibacterial effectors into rival bacterial cells. However, it has recently emerged that the T6SS can also be used as a powerful weapon against fungal competitors, and the first fungal-specific T6SS effector proteins, Tfe1 and Tfe2, have been identified. These effectors act via distinct mechanisms against a variety of fungal species to cause cell death. Tfe1 intoxication triggers plasma membrane depolarisation, whilst Tfe2 disrupts nutrient uptake and induces autophagy. Based on the frequent coexistence of bacteria and fungi in microbial communities, we propose that T6SS-dependent antifungal activity is likely to be widespread and elicited by a suite of antifungal effectors. Supporting this hypothesis, homologues of Tfe1 and Tfe2 are found in other bacterial species, and a number of T6SS-elaborating species have been demonstrated to interact with fungi. Thus, we envisage that antifungal T6SS will shape many polymicrobial communities, including the human microbiota and disease-causing infections.

12.
Nat Microbiol ; 3(8): 920-931, 2018 08.
Article in English | MEDLINE | ID: mdl-30038307

ABSTRACT

Interactions between bacterial and fungal cells shape many polymicrobial communities. Bacteria elaborate diverse strategies to interact and compete with other organisms, including the deployment of protein secretion systems. The type VI secretion system (T6SS) delivers toxic effector proteins into host eukaryotic cells and competitor bacterial cells, but, surprisingly, T6SS-delivered effectors targeting fungal cells have not been reported. Here we show that the 'antibacterial' T6SS of Serratia marcescens can act against fungal cells, including pathogenic Candida species, and identify the previously undescribed effector proteins responsible. These antifungal effectors, Tfe1 and Tfe2, have distinct impacts on the target cell, but both can ultimately cause fungal cell death. 'In competition' proteomics analysis revealed that T6SS-mediated delivery of Tfe2 disrupts nutrient uptake and amino acid metabolism in fungal cells, and leads to the induction of autophagy. Intoxication by Tfe1, in contrast, causes a loss of plasma membrane potential. Our findings extend the repertoire of the T6SS and suggest that antifungal T6SSs represent widespread and important determinants of the outcome of bacterial-fungal interactions.


Subject(s)
Antifungal Agents/pharmacology , Serratia marcescens/metabolism , Type VI Secretion Systems/pharmacology , Antifungal Agents/metabolism , Autophagy , Candida/drug effects , Gene Expression Regulation, Bacterial , Microbial Viability/drug effects , Proteomics , Type VI Secretion Systems/metabolism
13.
PLoS Pathog ; 14(7): e1007230, 2018 07.
Article in English | MEDLINE | ID: mdl-30052683

ABSTRACT

The Type VI secretion system (T6SS) is widely used by bacterial pathogens as an effective weapon against bacterial competitors and is also deployed against host eukaryotic cells in some cases. It is a contractile nanomachine which delivers toxic effector proteins directly into target cells by dynamic cycles of assembly and firing. Bacterial cells adopt distinct post-translational regulatory strategies for deployment of the T6SS. 'Defensive' T6SSs assemble and fire in response to incoming attacks from aggressive neighbouring cells, and can utilise the Threonine Protein Phosphorylation (TPP) regulatory pathway to achieve this control. However, many T6SSs are 'offensive', firing at all-comers without the need for incoming attack or other cell contact-dependent signal. Post-translational control of the offensive mode has been less well defined but can utilise components of the same TPP pathway. Here, we used the anti-bacterial T6SS of Serratia marcescens to elucidate post-translational regulation of offensive T6SS deployment, using single-cell microscopy and genetic analyses. We show that the integration of the TPP pathway with the negative regulator TagF to control core T6SS machine assembly is conserved between offensive and defensive T6SSs. Signal-dependent PpkA-mediated phosphorylation of Fha is required to overcome inhibition of membrane complex assembly by TagF, whilst PppA-mediated dephosphorylation promotes spatial reorientation and efficient killing. In contrast, the upstream input of the TPP pathway defines regulatory strategy, with a new periplasmic regulator, RtkS, shown to interact with the PpkA kinase in S. marcescens. We propose a model whereby the opposing actions of the TPP pathway and TagF impose a delay on T6SS re-assembly after firing, providing an opportunity for spatial re-orientation of the T6SS in order to maximise the efficiency of competitor cell targeting. Our findings provide a better understanding of how bacterial cells deploy competitive weapons effectively, with implications for the structure and dynamics of varied polymicrobial communities.


Subject(s)
Gene Expression Regulation, Bacterial/physiology , Protein Processing, Post-Translational/physiology , Serratia marcescens/metabolism , Serratia marcescens/pathogenicity , Type VI Secretion Systems/metabolism , Serratia marcescens/genetics , Type VI Secretion Systems/genetics
14.
Cell Rep ; 22(3): 774-785, 2018 01 16.
Article in English | MEDLINE | ID: mdl-29346773

ABSTRACT

Incorporation of disulfide bonds into proteins can be critical for function or stability. In bacterial cells, the periplasmic enzyme DsbA is responsible for disulfide incorporation into many extra-cytoplasmic proteins. The type VI secretion system (T6SS) is a widely occurring nanomachine that delivers toxic effector proteins directly into rival bacterial cells, playing a key role in inter-bacterial competition. We report that two redundant DsbA proteins are required for virulence and for proper deployment of the T6SS in the opportunistic pathogen Serratia marcescens, with several T6SS components being subject to the action of DsbA in secreting cells. Importantly, we demonstrate that DsbA also plays a critical role in recipient target cells, being required for the toxicity of certain incoming effector proteins. Thus we reveal that target cell functions can be hijacked by T6SS effectors for effector activation, adding a further level of complexity to the T6SS-mediated inter-bacterial interactions which define varied microbial communities.


Subject(s)
Bacterial Proteins/metabolism , Bacterial Secretion Systems/therapeutic use , Gene Expression Regulation, Bacterial/genetics , Type VI Secretion Systems/therapeutic use , Bacterial Secretion Systems/pharmacology , Type VI Secretion Systems/pharmacology
15.
Methods Mol Biol ; 1615: 517-524, 2017.
Article in English | MEDLINE | ID: mdl-28667634

ABSTRACT

Anti-bacterial activity assays are an important tool in the assessment of the ability of one bacterium to kill or inhibit the growth of another, for example during the study of the Type VI secretion system (T6SS) and the anti-bacterial toxins it secretes. The method we describe here can detect the ability of a bacterial strain to kill or inhibit other bacterial cells in a contact-dependent manner when co-cultured on an agar surface. It is particularly useful since it enumerates the recovery of viable target cells and thus enables quantification of the anti-bacterial activity. We provide a detailed description of how to measure the T6SS-dependent anti-bacterial activity of a bacterium such as Serratia marcescens against a competitor prokaryotic organism, Escherichia coli, and also describe possible variations in the method to allow adaptation to other attacker and target organisms.


Subject(s)
Anti-Bacterial Agents/toxicity , Antibiosis , Bacterial Physiological Phenomena , Bacterial Secretion Systems , Bacterial Toxins/toxicity , Coculture Techniques , Colony Count, Microbial
16.
PLoS Pathog ; 12(6): e1005735, 2016 06.
Article in English | MEDLINE | ID: mdl-27352036

ABSTRACT

The Type VI secretion system (T6SS) is widespread among bacterial pathogens and acts as an effective weapon against competitor bacteria and eukaryotic hosts by delivering toxic effector proteins directly into target cells. The T6SS utilises a bacteriophage-like contractile machinery to expel a puncturing device based on a tube of Hcp topped with a VgrG spike, which can be extended by a final tip from a PAAR domain-containing protein. Effector proteins are believed to be delivered by specifically associating with particular Hcp, VgrG or PAAR proteins, either covalently ('specialised') or non-covalently ('cargo' effectors). Here we used the T6SS of the opportunistic pathogen Serratia marcescens, together with integratecd genetic, proteomic and biochemical approaches, to elucidate the role of specific VgrG and PAAR homologues in T6SS function and effector specificity, revealing new aspects and unexpected subtleties in effector delivery by the T6SS. We identified effectors, both cargo and specialised, absolutely dependent on a particular VgrG for delivery to target cells, and discovered that other cargo effectors can show a preference for a particular VgrG. The presence of at least one PAAR protein was found to be essential for T6SS function, consistent with designation as a 'core' T6SS component. We showed that specific VgrG-PAAR combinations are required to assemble a functional T6SS and that the three distinct VgrG-PAAR assemblies in S. marcescens exhibit distinct effector specificity and efficiency. Unexpectedly, we discovered that two different PAAR-containing Rhs proteins can functionally pair with the same VgrG protein. Showing that accessory EagR proteins are involved in these interactions, native VgrG-Rhs-EagR complexes were isolated and specific interactions between EagR and cognate Rhs proteins identified. This study defines an essential yet flexible role for PAAR proteins in the T6SS and highlights the existence of distinct versions of the machinery with differential effector specificity and efficiency of target cell delivery.


Subject(s)
Bacterial Proteins/metabolism , Serratia marcescens/pathogenicity , Type VI Secretion Systems/metabolism , Amino Acid Sequence , Chromatography, Affinity , Coculture Techniques , Escherichia coli , Immunoblotting , Mass Spectrometry , Proteomics , Serratia marcescens/metabolism
17.
Trends Microbiol ; 24(1): 51-62, 2016 Jan.
Article in English | MEDLINE | ID: mdl-26549582

ABSTRACT

Bacteria utilise specialised protein secretion systems to interact with host organisms, competitor bacteria, and the environment. The Type VI secretion system (T6SS) is a versatile weapon deployed by many bacterial species to target either host cells or rival bacteria. The widespread occurrence and significance of the T6SS is becoming increasingly appreciated, as is its intriguing mode of action. The T6SS delivers multiple, diverse effector proteins directly into target cells using a dynamic 'firing' mechanism related to the action of contractile bacteriophage tails. Here, we summarise the contribution of recent findings to our developing picture of how the T6SS assembles and fires, how it is loaded with different types of effectors, and how it can be aimed towards an incoming assault.


Subject(s)
Bacteria/metabolism , Bacterial Proteins/physiology , Type VI Secretion Systems/physiology , Bacteriophages/physiology , Models, Molecular , Nanostructures/microbiology
19.
Cell Microbiol ; 17(12): 1742-51, 2015 Dec.
Article in English | MEDLINE | ID: mdl-26432982

ABSTRACT

The Type VI secretion system is a widespread bacterial nanomachine, used to deliver toxins directly into eukaryotic or prokaryotic target cells. These secreted toxins, or effectors, act on diverse cellular targets, and their action provides the attacking bacterial cell with a significant fitness advantage, either against rival bacteria or eukaryotic host organisms. In this review, we discuss the delivery of diverse effectors by the Type VI secretion system, the modes of action of the so-called 'anti-bacterial' and 'anti-eukaryotic' effectors, the mechanism of self-resistance against anti-bacterial effectors and the evolutionary implications of horizontal transfer of Type VI secretion system-associated toxins. Whilst it is likely that many more effectors remain to be identified, it is already clear that toxins delivered by this secretion system represent efficient weapons against both bacteria and eukaryotes.


Subject(s)
Bacteria/pathogenicity , Bacterial Toxins/metabolism , Eukaryotic Cells/microbiology , Eukaryotic Cells/physiology , Type VI Secretion Systems/metabolism , Virulence Factors/metabolism , Antibiosis , Bacteria/metabolism , Cell Survival/drug effects , Microbial Viability/drug effects , Virulence
20.
Cell Rep ; 12(12): 2131-42, 2015 Sep 29.
Article in English | MEDLINE | ID: mdl-26387948

ABSTRACT

The Type VI secretion system (T6SS) is a bacterial nanomachine that fires toxic proteins into target cells. Deployment of the T6SS represents an efficient and widespread means by which bacteria attack competitors or interact with host organisms and may be triggered by contact from an attacking neighbor cell as a defensive strategy. Here, we use the opportunist pathogen Serratia marcescens and functional fluorescent fusions of key components of the T6SS to observe different subassemblies of the machinery simultaneously and on multiple timescales in vivo. We report that the localization and dynamic behavior of each of the components examined is distinct, revealing a multi-stage and dynamic assembly process for the T6SS machinery. We also show that the T6SS can assemble and fire without needing a cell contact trigger, defining an aggressive strategy that broadens target range and suggesting that activation of the T6SS is tailored to survival in specific niches.


Subject(s)
Bacterial Proteins/genetics , Gene Expression Regulation, Bacterial , Serratia marcescens/genetics , Type VI Secretion Systems/genetics , Bacterial Proteins/metabolism , Green Fluorescent Proteins/genetics , Green Fluorescent Proteins/metabolism , Kinetics , Luminescent Proteins/genetics , Luminescent Proteins/metabolism , Microscopy, Fluorescence , Multigene Family , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Serratia marcescens/metabolism , Serratia marcescens/ultrastructure , Type VI Secretion Systems/metabolism , Type VI Secretion Systems/ultrastructure , Red Fluorescent Protein
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