Výsledky vyhledávání - "Thiago E. Rodrigues"

Fatty acid biosynthesis is enhanced in Escherichia coli strains with deletion in genes encoding the PII signaling proteins

Autor: Thiago E. Rodrigues, Glaucio Valdameri, Guilherme L. Sassaki, Luciano F. Huergo, Emanuel Maltempi de Souza, Fábio O. Pedrosa

Publikováno v: Archives of microbiology. 201(2)

The committed and rate-limiting step in fatty acid biosynthesis is catalyzed by acetyl-CoA carboxylase (ACC). In previous studies we showed that ACC activity is inhibited through interactions with the PII signaling proteins in vitro. Here we provide

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c99423a6b84807c100d79e3428015bb7
https://pubmed.ncbi.nlm.nih.gov/30506165

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The Bacterial signal transduction protein GlnB regulates the committed step in fatty acid biosynthesis by acting as a dissociable regulatory subunit of acetyl-CoA carboxylase

Autor: Thiago E. Rodrigues, Karl Forchhammer, Luciano F. Huergo, Emanuel Maltempi de Souza, Marcelo Müller-Santos, Edileusa C. M. Gerhardt, Fábio O. Pedrosa

Publikováno v: Molecular Microbiology. 95:1025-1035

Biosynthesis of fatty acids is one of the most fundamental biochemical pathways in nature. In bacteria and plant chloroplasts, the committed and rate-limiting step in fatty acid biosynthesis is catalyzed by a multi-subunit form of the acetyl-CoA carb

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https://doi.org/10.1111/mmi.12912

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Proteome analysis of an Escherichia coli ptsN-null strain under different nitrogen regimes

Autor: Glaucio Valdameri, Heloisa B.S. Sanchuki, Fábio O. Pedrosa, Fernanda Gravina, Gustavo A. de Souza, Thiago E. Rodrigues, Luciano F. Huergo, Emanuel Maltempi de Souza, Edileusa C. M. Gerhardt

Publikováno v: Journal of proteomics. 174

The carbohydrate-uptake phosphorelay PTS system plays a key role in metabolic regulation in Bacteria controlling the utilization of secondary carbon sources. Some bacteria, such as Escherichia coli, encode a paralogous system named PTSNtr (nitrogen r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95eab7e057cfc4fb695cd67b046e988c
https://pubmed.ncbi.nlm.nih.gov/29274402

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Search for novel targets of the PIIsignal transduction protein in Bacteria identifies the BCCP component of acetyl-CoA carboxylase as a PIIbinding partner

Autor: Gustavo A. Souza, Leda S. Chubatsu, Luciano F. Huergo, Emanuel Maltempi de Souza, Edileusa C. M. Gerhardt, Marcelo Müller-Santos, Thiago E. Rodrigues, Fábio O. Pedrosa, Marco A. S. Oliveira

Publikováno v: Molecular Microbiology. 91:751-761

Summary The PII family comprises a group of widely distributed signal transduction proteins. The archetypal function of PII is to regulate nitrogen metabolism in bacteria. As PII can sense a range of metabolic signals, it has been suggested that the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::79d6175a005d8dc92f2dcd9510c14c40
https://doi.org/10.1111/mmi.12493

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Dynamics of the Escherichia coli proteome in response to nitrogen starvation and entry into the stationary phase

Autor: Gustavo A. de Souza, Fábio O. Pedrosa, Glaucio Valdameri, Heloisa B.S. Sanchuki, Thiago E. Rodrigues, Luciano F. Huergo, Emanuel Maltempi de Souza, Edileusa C. M. Gerhardt, Fernanda Gravina, Roberto Tadeu Raittz

Publikováno v: Biochimica et biophysica acta. Proteins and proteomics. 1865(3)

Nitrogen is needed for the biosynthesis of biomolecules including proteins and nucleic acids. In the absence of fixed nitrogen prokaryotes such as E. coli immediately ceases growth. Ammonium is the preferred nitrogen source for E. coli supporting the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2de5523c93331f91431d62d1f0075c25
https://pubmed.ncbi.nlm.nih.gov/27939605

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The bacterial signal transduction protein GlnB regulates the committed step in fatty acid biosynthesis by acting as a dissociable regulatory subunit of acetyl-CoA carboxylase

Autor: Edileusa C M, Gerhardt, Thiago E, Rodrigues, Marcelo, Müller-Santos, Fabio O, Pedrosa, Emanuel M, Souza, Karl, Forchhammer, Luciano F, Huergo

Publikováno v: Molecular microbiology. 95(6)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::61cb6e9c90a47bda15a5322079ecc10f
https://pubmed.ncbi.nlm.nih.gov/25557370

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Search for novel targets of the PII signal transduction protein in Bacteria identifies the BCCP component of acetyl-CoA carboxylase as a PII binding partner

Autor: Thiago E, Rodrigues, Edileusa C M, Gerhardt, Marco A, Oliveira, Leda S, Chubatsu, Fabio O, Pedrosa, Emanuel M, Souza, Gustavo A, Souza, Marcelo, Müller-Santos, Luciano F, Huergo

Publikováno v: Molecular microbiology. 91(4)

The PII family comprises a group of widely distributed signal transduction proteins. The archetypal function of PII is to regulate nitrogen metabolism in bacteria. As PII can sense a range of metabolic signals, it has been suggested that the number o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d8dee162dc39eae262d6761f7e363bae
https://pubmed.ncbi.nlm.nih.gov/24329683

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Influence of the ADP/ATP ratio, 2-oxoglutarate and divalent ions on Azospirillum brasilense PII protein signalling

Autor: Rose A. Monteiro, Ronny R. Ribeiro, Edileusa C. M. Gerhardt, Thiago E. Rodrigues, Fábio O. Pedrosa, Marcelo Scarduelli, Luíza M. Araújo, Luciano F. Huergo, Emanuel Maltempi de Souza, Leda S. Chubatsu

Publikováno v: Microbiology (Reading, England). 158(Pt 6)

Proteins belonging to the P(II) family coordinate cellular nitrogen metabolism by direct interaction with a variety of enzymes, transcriptional regulators and transporters. The sensing function of P(II) relies on its ability to bind the nitrogen/carb

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5a470bbc233d2516b937b7641dfad59
https://pubmed.ncbi.nlm.nih.gov/22461486

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In vitro interaction between the ammonium transport protein AmtB and partially uridylylated forms of the PII protein GlnZ

Autor: Leda S. Chubatsu, Luíza M. Araújo, Luciano F. Huergo, Victor E.P. Souza, Emanuel Maltempi de Souza, Edileusa C. M. Gerhardt, Rose A. Monteiro, Thiago E. Rodrigues, Fábio O. Pedrosa

Publikováno v: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. (9):1203-1209

The ammonium transport family Amt/Rh comprises ubiquitous integral membrane proteins that facilitate ammonium movement across biological membranes. Besides their role in transport, Amt proteins also play a role in sensing the levels of ammonium in th

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