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Outputs (14)

The Quorum Sensing Auto-Inducer 2 (AI-2) Stimulates Nitrogen Fixation and Favors Ethanol Production over Biomass Accumulation in Zymomonas mobilis (2021)
Journal Article
Alencar, V. C., Silva, J. D. F. D. S., Vilas Boas, R. O., Farnézio, V. M., de Maria, Y. N., Aciole Barbosa, D., Almeida, A. T., de Souza, E. M., Müller-Santos, M., Jabes, D. L., Menegidio, F. B., Costa de Oliveira, R., Rodrigues, T., Tersariol, I. L. D. S., Walmsley, A. R., & Nunes, L. R. (2021). The Quorum Sensing Auto-Inducer 2 (AI-2) Stimulates Nitrogen Fixation and Favors Ethanol Production over Biomass Accumulation in Zymomonas mobilis. International Journal of Molecular Sciences, 22(11), https://doi.org/10.3390/ijms22115628

Autoinducer 2 (or AI-2) is one of the molecules used by bacteria to trigger the Quorum Sensing (QS) response, which activates expression of genes involved in a series of alternative mechanisms, when cells reach high population densities (including bi... Read More about The Quorum Sensing Auto-Inducer 2 (AI-2) Stimulates Nitrogen Fixation and Favors Ethanol Production over Biomass Accumulation in Zymomonas mobilis.

Zmo0994, a novel LEA-like protein from Zymomonas mobilis, increases multi-abiotic stress tolerance in Escherichia coli (2020)
Journal Article
Yang, J., Kim, H. E., Jung, Y. H., Kim, J., Kim, D. H., Walmsley, A. R., & Kim, K. H. (2020). Zmo0994, a novel LEA-like protein from Zymomonas mobilis, increases multi-abiotic stress tolerance in Escherichia coli. Biotechnology for Biofuels, 13(1), Article 151. https://doi.org/10.1186/s13068-020-01790-0

Background: Pretreatment processes and subsequent enzymatic hydrolysis are prerequisites to utilize lignocellulosic sugar for fermentation. However, the resulting hydrolysate frequently hinders fermentation processes due to the presence of inhibitors... Read More about Zmo0994, a novel LEA-like protein from Zymomonas mobilis, increases multi-abiotic stress tolerance in Escherichia coli.

The Vibrio cholerae var regulon encodes a metallo-β-lactamase and an antibiotic efflux pump, which are regulated by VarR, a LysR-type transcription factor (2017)
Journal Article
Lin, H. V., Massam-Wu, T., Lin, C., Wang, Y. A., Shen, Y., Lu, W., …Walmsley, A. R. (2017). The Vibrio cholerae var regulon encodes a metallo-β-lactamase and an antibiotic efflux pump, which are regulated by VarR, a LysR-type transcription factor. PLoS ONE, 12(9), Article e0184255. https://doi.org/10.1371/journal.pone.0184255

The genome sequence of V. cholerae O1 Biovar Eltor strain N16961 has revealed a putative antibiotic resistance (var) regulon that is predicted to encode a transcriptional activator (VarR), which is divergently transcribed relative to the putative res... Read More about The Vibrio cholerae var regulon encodes a metallo-β-lactamase and an antibiotic efflux pump, which are regulated by VarR, a LysR-type transcription factor.

A Gβ protein and the TupA Co-Regulator Bind to Protein Kinase A Tpk2 to Act as Antagonistic Molecular Switches of Fungal Morphological Changes (2015)
Journal Article
Janganan, T., Chen, G., Chen, D., Menino, J., Rodrigues, F., Borges-Walmsley, M., & Walmsley, A. (2015). A Gβ protein and the TupA Co-Regulator Bind to Protein Kinase A Tpk2 to Act as Antagonistic Molecular Switches of Fungal Morphological Changes. PLoS ONE, 10(9), Article e0136866. https://doi.org/10.1371/journal.pone.0136866

The human pathogenic fungus Paracoccidioides brasiliensis (Pb) undergoes a morphological transition from a saprobic mycelium to pathogenic yeast that is controlled by the cAMP-signaling pathway. There is a change in the expression of the Gβ-protein P... Read More about A Gβ protein and the TupA Co-Regulator Bind to Protein Kinase A Tpk2 to Act as Antagonistic Molecular Switches of Fungal Morphological Changes.

Tripartite efflux pumps: energy is required for dissociation, but not assembly or opening of the outer membrane channel of the pump (2013)
Journal Article
Janganan, T., Bavro, V., Zhang, L., Borges-Walmsley, M., & Walmsley, A. (2013). Tripartite efflux pumps: energy is required for dissociation, but not assembly or opening of the outer membrane channel of the pump. Molecular Microbiology, 88(3), 590-602. https://doi.org/10.1111/mmi.12211

The MtrCDE multidrug pump, from Neisseria gonorrhoeae, is assembled from the inner and outer membrane proteins MtrD and MtrE, which are connected by the periplasmic membrane fusion protein MtrC. Although it is clear that MtrD delivers drugs to the ch... Read More about Tripartite efflux pumps: energy is required for dissociation, but not assembly or opening of the outer membrane channel of the pump.

Evidence for the assembly of a bacterial tripartite multidrug pump with a stoichiometry of 3:6:3 (2011)
Journal Article
Janganan, T., Bavro, V., Zhang, L., Matak-Vinkovic, D., Barrera, N., Venien-Bryan, C., …Walmsley, A. (2011). Evidence for the assembly of a bacterial tripartite multidrug pump with a stoichiometry of 3:6:3. Journal of Biological Chemistry, 286(30), 26900-26912. https://doi.org/10.1074/jbc.m111.246595

The multiple transferable resistance (mTR) pump from Neisseria gonorrhoeae MtrCDE multidrug pump is assembled from the inner and outer membrane proteins MtrD and MtrE and the periplasmic membrane fusion protein MtrC. Previously we established that wh... Read More about Evidence for the assembly of a bacterial tripartite multidrug pump with a stoichiometry of 3:6:3.

Opening of the Outer Membrane Protein Channel in Tripartite Efflux Pumps Is Induced by Interaction with the Membrane Fusion Partner (2011)
Journal Article
Janganan, T., Zhang, L., Bavro, V., Matak-Vinkovic, D., Barrera, N., Burton, M., …Walmsley, A. (2011). Opening of the Outer Membrane Protein Channel in Tripartite Efflux Pumps Is Induced by Interaction with the Membrane Fusion Partner. Journal of Biological Chemistry, 286(7), 5484-5493. https://doi.org/10.1074/jbc.m110.187658

The multiple transferable resistance (MTR) pump, from Neisseria gonorrhoeae, is typical of the specialized machinery used to translocate drugs across the inner and outer membranes of Gram-negative bacteria. It consists of a tripartite complex compose... Read More about Opening of the Outer Membrane Protein Channel in Tripartite Efflux Pumps Is Induced by Interaction with the Membrane Fusion Partner.

MacB ABC transporter is a dimer whose ATPase activity and macrolide-binding capacity are regulated by the membrane fusion protein MacA (2009)
Journal Article
Lin, H., Bavro, V., Barrera, N., Frankish, H., Velamakanni, S., van Veen, H., …Walmsley, A. (2009). MacB ABC transporter is a dimer whose ATPase activity and macrolide-binding capacity are regulated by the membrane fusion protein MacA. Journal of Biological Chemistry, 284(2), 1145-1154. https://doi.org/10.1074/jbc.m806964200

Gram-negative bacteria utilize specialized machinery to translocate drugs and protein toxins across the inner and outer membranes, consisting of a tripartite complex composed of an inner membrane secondary or primary active transporter (IMP), a perip... Read More about MacB ABC transporter is a dimer whose ATPase activity and macrolide-binding capacity are regulated by the membrane fusion protein MacA.

An arsenic metallochaperone for an arsenic detoxification pump (2006)
Journal Article
Lin, Y., Walmsley, A. R., & Rosen, B. P. (2006). An arsenic metallochaperone for an arsenic detoxification pump. Proceedings of the National Academy of Sciences, 103(42), 15617-15622. https://doi.org/10.1073/pnas.0603974103

Environmental arsenic is a world-wide health issue, making it imperative for us to understand mechanisms of metalloid uptake and detoxification. The predominant intracellular form is the highly mephitic arsenite, which is detoxified by removal from c... Read More about An arsenic metallochaperone for an arsenic detoxification pump.

The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 Å resolution (2005)
Journal Article
Federici, L., Du, D., Walas, F., Matsumura, H., Fernandez-Recio, J., McKeegan, K. S., Borges-Walmsley, M. I., Luisi, B. F., & Walmsley, A. R. (2005). The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 Å resolution. Journal of Biological Chemistry, 280(15), 15307-15314. https://doi.org/10.1074/jbc.m500401200

Multidrug resistance in Gram-negative bacteria arises in part from the activities of tripartite drug efflux pumps. In the pathogen Vibrio cholerae, one such pump comprises the inner membrane proton antiporter VceB, the periplasmic adaptor VceA, and t... Read More about The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 Å resolution.

Identification of oligomerization and drug-binding domains of the membrane fusion protein EmrA (2002)
Journal Article
Borges-Walmsley, M., Beauchamp, J., Kelly, S., Jumel, K., Candlish, D., Harding, S., …Walmsley, A. (2003). Identification of oligomerization and drug-binding domains of the membrane fusion protein EmrA. Journal of Biological Chemistry, 278(15), 12903-12912. https://doi.org/10.1074/jbc.m209457200

Many pathogenic Gram-negative bacteria possess tripartite transporters that catalyze drug extrusion across the inner and outer membranes, thereby conferring resistance. These transporters consist of inner (IMP) and outer (OMP) membrane proteins, whic... Read More about Identification of oligomerization and drug-binding domains of the membrane fusion protein EmrA.

Evidence for Cooperativity between the Four Binding Sites of Dimeric ArsD, an As (III)-responsive Transcriptional Regulator (2002)
Journal Article
Song, L., Rosen, B., Borges-Walmsley, M., & Walmsley, A. (2002). Evidence for Cooperativity between the Four Binding Sites of Dimeric ArsD, an As (III)-responsive Transcriptional Regulator. Journal of Biological Chemistry, 277(29), 25992-26002. https://doi.org/10.1074/jbc.m201619200

ArsD is a trans-acting repressor of the arsRDABC operon that confers resistance to arsenicals and antimonials in Escherichia coli. It possesses two-pairs of vicinal cysteine residues, Cys12-Cys13 and Cys112-Cys113, that potentially form separate bind... Read More about Evidence for Cooperativity between the Four Binding Sites of Dimeric ArsD, an As (III)-responsive Transcriptional Regulator.

A kinetic model for the action of a resistance efflux pump (2001)
Journal Article
Walmsley, A., Zhou, T., Borges-Walmsley, M., & Rosen, B. (2001). A kinetic model for the action of a resistance efflux pump. Journal of Biological Chemistry, 276(9), 6378-6391. https://doi.org/10.1074/jbc.m008105200

ArsA is the catalytic subunit of the arsenical pump, coupling ATP hydrolysis to the efflux of arsenicals through the ArsB membrane protein. It is a paradigm for understanding the structure-function of the nucleotide binding domains (NBD) of medically... Read More about A kinetic model for the action of a resistance efflux pump.