Comprehensive analysis of transport proteins encoded within the genome of Bdellovibrio bacteriovorus

Barabote, Ravi D.; Rendulic, Snjezana; Schuster, Stephan C.; Saier, Milton H.

doi:10.1016/j.ygeno.2007.06.002

Cited by 29 publications

(29 citation statements)

References 135 publications

(173 reference statements)

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“…Type III and type IV secretion systems are absent. Protein secretion into the prey cytoplasm is probably first accomplished via secretion into the prey periplasm and then by retrotranslocation into the host cytoplasm (Barabote et al 2007). Another peculiar mechanism is the embedding by B. bacteriovorus of predator OMPs onto the prey cytoplasmic membrane, probably permeabilizing it to small hydrophilic molecules (Barel et al 2005;Beck et al 2004).…”

Section: Transportmentioning

confidence: 99%

“…Some of the system's components are specifically expressed during particular phases of the cell cycle and appear to promote the transfer of proteins to the prey cytoplasm (Chang et al 2011). BALO genomes encode for unusually large inventories of transport systems (Barabote et al 2007). The d-proteobacteria Bdellovibrionaceae and Bacteriovoracaceae bear numerous uptake systems for amino acids and peptides; in contrast, none is detected in the epibiotic a-proteobacteria Micavibrio aeruginosavorus (Hobley et al 2012b;Rendulic et al 2004;Wang et al 2011).…”

Section: Transportmentioning

confidence: 99%

“…B. bacteriovorus has three sugar permeases, enabling the import of ribose, glycosides, maltose, and malto-oligosaccharides (Hespell et al 1973). In contrast, many efflux pumps are found (Barabote et al 2007). The phosphoenolpyruvate-dependent sugar transporting phosphotransferase system (PTS) is absent.…”

Section: Transportmentioning

confidence: 99%

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Bdellovibrio and Like Organisms

2014

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Section: Transportmentioning

confidence: 99%

Section: Transportmentioning

confidence: 99%

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Bdellovibrio and Like Organisms

2014

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“…This outer membrane protein is the pore protein through which folded polypeptides are secreted to the extracellular space through a type II secretion pathway (47). B. bacteriovorus has no known syringe-like secretion systems; most probably, the majority of the very large complement of its secreted proteins is exported through the Sec pathway (48). At this stage, we can only hypothesize that c-di-GMP modulation affects GspD while in the cytoplasm, perhaps by controlling its own secretion through interactions with other components of the secretion machinery.…”

Section: Discussionmentioning

confidence: 99%

An Extended Cyclic Di-GMP Network in the Predatory Bacterium Bdellovibrio bacteriovorus

et al. 2016

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Over the course of the last 3 decades the role of the second messenger cyclic di-GMP (c-di-GMP) as a master regulator of bacterial physiology was determined. Although the control over c-di-GMP levels via synthesis and breakdown and the allosteric regulation of c-di-GMP over receptor proteins (effectors) and riboswitches have been extensively studied, relatively few effectors have been identified and most are of unknown functions. The obligate predatory bacterium Bdellovibrio bacteriovorus has a peculiar dimorphic life cycle, in which a phenotypic transition from a free-living attack phase (AP) to a sessile, intracellular predatory growth phase (GP) is tightly regulated by specific c-di-GMP diguanylate cyclases. B. bacteriovorus also bears one of the largest complement of defined effectors, almost none of known functions, suggesting that additional proteins may be involved in c-di-GMP signaling. In order to uncover novel c-di-GMP effectors, a c-di-GMP capture-compound mass-spectroscopy experiment was performed on wild-type AP and host-independent (HI) mutant cultures, the latter serving as a proxy for wild-type GP cells. Eightyfour proteins were identified as candidate c-di-GMP binders. Of these proteins, 65 did not include any recognized c-di-GMP binding site, and 3 carried known unorthodox binding sites. Putative functions could be assigned to 59 proteins. These proteins are included in metabolic pathways, regulatory circuits, cell transport, and motility, thereby creating a potentially large c-di-GMP network. False candidate effectors may include members of protein complexes, as well as proteins binding nucleotides or other cofactors that were, respectively, carried over or unspecifically interacted with the capture compound during the pulldown. Of the 84 candidates, 62 were found to specifically bind the c-di-GMP capture compound in AP or in HI cultures, suggesting c-di-GMP control over the whole-cell cycle of the bacterium. High affinity and specificity to c-di-GMP binding were confirmed using microscale thermophoresis with a hypothetical protein bearing a PilZ domain, an acyl coenzyme A dehydrogenase, and a two-component system response regulator, indicating that additional c-di-GMP binding candidates may be bona fide novel effectors. IMPORTANCEIn this study, 84 putative c-di-GMP binding proteins were identified in B. bacteriovorus, an obligate predatory bacterium whose lifestyle and reproduction are dependent on c-di-GMP signaling, using a c-di-GMP capture compound precipitation approach. This predicted complement covers metabolic, energy, transport, motility and regulatory pathways, and most of it is phase specific, i.e., 62 candidates bind the capture compound at defined modes of B. bacteriovorus lifestyle. Three of the putative binders further demonstrated specificity and high affinity to c-di-GMP via microscale thermophoresis, lending support for the presence of additional bona fide c-di-GMP effectors among the pulled-down protein repertoire.

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“…Subsequent genome sequencing and analysis of a related strain of B. bacteriovorus, type strain HD100 (2,21), showed there to be three sets of motAB genes, Bd0144-Bd0145, Bd3021-Bd3020, and Bd3254-Bd3253, along with gene duplication of many other vital components of the flagellar structure, including six copies of the filament subunit gene fliC (10,13) and two copies of the rotor component gene fliG (14), although not enough duplicated components to encode a fully alternate flagellar structure. The Bd0144 motA gene of B. bacteriovorus HD100 showed 100% identity, at DNA and protein levels, to the motA gene in B. bacteriovorus 109J described by Flannagan et al (8), and there was also synteny with its surrounding genetic locus, including motB, between the two strains.…”

mentioning

confidence: 99%

Three motAB Stator Gene Products in Bdellovibrio bacteriovorus Contribute to Motility of a Single Flagellum during Predatory and Prey-Independent Growth

et al. 2011

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The predatory bacterium Bdellovibrio bacteriovorus uses flagellar motility to locate regions rich in Gramnegative prey bacteria, colliding and attaching to prey and then ceasing flagellar motility. Prey are then invaded to form a "bdelloplast" in a type IV pilus-dependent process, and prey contents are digested, allowing Bdellovibrio growth and septation. After septation, Bdellovibrio flagellar motility resumes inside the prey bdelloplast prior to its lysis and escape of Bdellovibrio progeny. Bdellovibrio can also grow slowly outside prey as long flagellate host-independent (

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Comprehensive analysis of transport proteins encoded within the genome of Bdellovibrio bacteriovorus

Cited by 29 publications

References 135 publications

Bdellovibrio and Like Organisms

Bdellovibrio and Like Organisms

An Extended Cyclic Di-GMP Network in the Predatory Bacterium Bdellovibrio bacteriovorus

Three motAB Stator Gene Products in Bdellovibrio bacteriovorus Contribute to Motility of a Single Flagellum during Predatory and Prey-Independent Growth

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