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23 results on '"Muriel-Millán, Luis Felipe"'

11. Characterization of a Novel Functional Trimeric Catechol 1,2-Dioxygenase From a Pseudomonas stutzeri Isolated From the Gulf of Mexico

Author

Rodríguez-Salazar, Julieta, primary, Almeida-Juarez, Arisbeth G., additional, Ornelas-Ocampo, Katya, additional, Millán-López, Sofía, additional, Raga-Carbajal, Enrique, additional, Rodríguez-Mejía, José Luis, additional, Muriel-Millán, Luis Felipe, additional, Godoy-Lozano, E. Ernestina, additional, Rivera-Gómez, Nancy, additional, Rudiño-Piñera, Enrique, additional, and Pardo-López, Liliana, additional

Published
2020
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13. Functional and Genomic Characterization of a Pseudomonas aeruginosa Strain Isolated From the Southwestern Gulf of Mexico Reveals an Enhanced Adaptation for Long-Chain Alkane Degradation

Author

Muriel-Millán, Luis Felipe, primary, Rodríguez-Mejía, José Luis, additional, Godoy-Lozano, Elizabeth Ernestina, additional, Rivera-Gómez, Nancy, additional, Gutierrez-Rios, Rosa-María, additional, Morales-Guzmán, Daniel, additional, Trejo-Hernández, María R., additional, Estradas-Romero, Alejandro, additional, and Pardo-López, Liliana, additional

Published
2019
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14. Two-component system CbrA/CbrB controls alginate production in Azotobacter vinelandii

Author

Quiroz-Rocha, Elva, primary, Bonilla-Badía, Fernando, additional, García-Aguilar, Valentina, additional, López-Pliego, Liliana, additional, Serrano-Román, Jade, additional, Cocotl-Yañez, Miguel, additional, Guzmán, Josefina, additional, Ahumada-Manuel, Carlos L., additional, Muriel-Millán, Luis Felipe, additional, Castañeda, Miguel, additional, Espín, Guadalupe, additional, and Nuñez, Cinthia, additional

Published
2017
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20. Unphosphorylated EIIANtr induces Clp AP-mediated degradation of Rpo S in A zotobacter vinelandii.

Author

Muriel‐Millán, Luis Felipe, Moreno, Soledad, Gallegos‐Monterrosa, Ramsés, and Espín, Guadalupe

Subjects
*PHOSPHOTRANSFERASES, *TRANSFERASES, *GRAM-negative bacteria, *SOIL microbiology, *PROTEOLYTIC enzymes
Abstract

The nitrogen-related phosphotransferase system (PTSNtr) is composed of the EINtr, NPr and EIIANtr proteins that form a phosphorylation cascade from phosphoenolpyruvate. PTSNtr is a global regulatory system present in most Gram-negative bacteria that controls some pivotal processes such as potassium and phosphate homeostasis, virulence, nitrogen fixation and ABC transport activation. In the soil bacterium Azotobacter vinelandii, unphosphorylated EIIANtr negatively regulates the expression of genes related to the synthesis of the bioplastic polyester poly-β-hydroxybutyrate (PHB) and cyst-specific lipids alkylresorcinols (ARs). The mechanism by which EIIANtr controls gene expression in A. vinelandii is not known. Here, we show that, in presence of unphosphorylated EIIANtr, the stability of the stationary phase sigma factor RpoS, which is necessary for transcriptional activation of PHB and ARs synthesis related genes, is reduced, and that the inactivation of genes coding for ClpAP protease complex in strains that carry unphosphorylated EIIANtr, restored the levels and in vivo stability of RpoS, as well as the synthesis of PHB and ARs. Taken together, our results reveal a novel mechanism, by which EIIANtr globally controls gene expression in A. vinelandii, where the unphosphorylated EIIANtr induces the degradation of RpoS by the proteolytic complex ClpAP. [ABSTRACT FROM AUTHOR]

Published
2017
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23. The Unphosphorylated EIIANtr Protein Represses the Synthesis of Alkylresorcinols in Azotobacter vinelandii.

Author

Muriel-Millán, Luis Felipe, Moreno, Soledad, Romero, Yanet, Bedoya-Pérez, Leidy Patricia, Castañeda, Miguel, Segura, Daniel, and Espín, Guadalupe

Subjects
*PHOSPHORYLATION, *PROTEIN synthesis, *RESORCINOL, *AZOTOBACTER vinelandii, *LIPIDS
Abstract

Upon encystment induction, Azotobacter vinelandii produces the phenolic lipids alkylresorcinols (ARs) that are structural components of the cysts. The enzymes responsible for the ARs synthesis are encoded in the arsABCD operon, whose expression is activated by ArpR. The transcription of arpR is initiated from an RpoS dependent promoter. The nitrogen-related phosphotransferase system (PTSNtr) is a global regulatory system present in Gram negative bacteria. It comprises the EINtr, NPr and EIIANtr proteins encoded by ptsP, ptsO and ptsN genes respectively. These proteins participate in a phosphoryl-group transfer from phosphoenolpyruvate to protein EIIANtr via the phosphotransferases EINtr and NPr. In A. vinelandii, the non-phosphorylated form of EIIANtr was previously shown to repress the synthesis of poly-ß-hydroxybutyrate. In this work, we show that PTSNtr also regulates the synthesis of ARs. In a strain that carries unphosphorylated EIIANtr, the expression of arpR was reduced, while synthesis of ARs and transcription of arsA were almost abrogated. The expression of arpR from an RpoS-independent promoter in this strain restored the ARs synthesis. Taken together these results indicate that unphosphorylated EIIANtr negatively affects activation of arpR transcription by RpoS. [ABSTRACT FROM AUTHOR]

Published
2015
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