Bacterial Protein Secretion Systems

Jiménez‐Guerrero, Irene; Cubo, MT; Pérez‐Montaño, Francisco; López‐Baena, Francisco Javier; Guash-Vidal, B; Ollero, Francisco Javier; Bellogín, Ramón A.; Espuny, M. Rosario

doi:10.1201/b15251-10

Cited by 2 publications

(1 citation statement)

References 156 publications

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“…PhoA is an enzyme that only folds correctly and presents activity if exported to the periplasm of E. coli, where disulfide bonds can be formed. In the presence of a specific substrate such as 5bromo-4-chloro-3-indolyl phosphate (X-Pho), colonies expression PhoA in the periplasm develop a blue color, while colonies whose enzyme is expressed in the cytoplasm remains white (Jiménez-Guerrero et al, 2013). Conversely, GFPuv only fluoresces in the cytoplasm since the oxidizing environment in the periplasm promotes the formation of disulfide bonds between C49 and C71, which causes misfolding, impeding chromophore maturation (Dammeyer and Tinnefeld, 2012).…”

Section: Topology Of Pga Synthetase Subunitsmentioning

confidence: 99%

Characterization of a membrane enzymatic complex for heterologous production of poly-γ-glutamate inE. coli

Nascimento

Nair

2020

Preprint

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Poly-γ-glutamic acid (PGA) produced by many Bacillus species is a polymer with many distinct and desirable characteristics. However, the multi-subunit enzymatic complex responsible for its synthesis, PGA Synthetase (PGS), has not been well characterized yet, in native nor in recombinant contexts. Elucidating structural and functional properties are crucial for future engineering efforts aimed at altering the catalytic properties of this enzyme. This study focuses on expressing the enzyme heterologously in the Escherichia coli membrane and characterizing localization, orientation, and activity of this heterooligomeric enzyme complex. In E. coli, we were able to produce high molecular weight PGA polymers with minimal degradation at titers of approximately 13 mg/L in deep-well microtiter batch cultures. Using fusion proteins, we observed, for the first time, the association and orientation of the different subunits with the inner cell membrane. These results elucidate provide fundamental structural information on this poorly studied enzyme complex and will aid future fundamental studies and engineering efforts.

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Section: Topology Of Pga Synthetase Subunitsmentioning

confidence: 99%

Characterization of a membrane enzymatic complex for heterologous production of poly-γ-glutamate inE. coli

Nascimento

Nair

2020

Preprint

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The Azospirillum brasilense type VI secretion system promotes cell aggregation, biocontrol protection against phytopathogens and attachment to the microalgae Chlorella sorokiniana

Cassán

Coniglio

Amavizca³

et al. 2021

Environmental Microbiology

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The plant-growth-promoting bacterium Azospirillum brasilense is able to associate with the microalgae Chlorella sorokiniana. Attachment of A. brasilense increases the metabolic performances of the microalgae. Recent genome analyses have revealed that the A. brasilense Az39 genome contains two complete sets of genes encoding type VI secretion systems (T6SS), including the T6SS1 that is induced by the indole-3-acetic acid (IAA) phytohormone. The T6SS is a multiprotein machine, widespread in Gramnegative bacteria, that delivers protein effectors in both prokaryotic and eukaryotic cells. Here we show that the A. brasilense T6SS is required for Chlorella-Azospirillum synthetic mutualism. Our data demonstrate that the T6SS is an important determinant to promote production of lipids, carbohydrates and photosynthetic pigments by the microalgae. We further show that this is likely due to the role of the T6SS during the attachment stage and for the production of IAA phytohormones. Finally, we demonstrate that the A. brasilense T6SS provides antagonistic activities against a number of plant pathogens such as Agrobacterium, Pectobacterium, Dickeya and Ralstonia species in vitro, suggesting that, in addition to promoting growth, A. brasilense might confer T6SS-dependent bio-control protection to microalgae and plants against bacterial pathogens.

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Bacterial Protein Secretion Systems

Cited by 2 publications

References 156 publications

Characterization of a membrane enzymatic complex for heterologous production of poly-γ-glutamate inE. coli

Characterization of a membrane enzymatic complex for heterologous production of poly-γ-glutamate inE. coli

The Azospirillum brasilense type VI secretion system promotes cell aggregation, biocontrol protection against phytopathogens and attachment to the microalgae Chlorella sorokiniana

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