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Different responses of the GlnB and GlnZ proteins upon in vitro uridylylation by the Azospirillum brasilense GlnD protein
Araújo, L. M; Huergo, L. F; Invitti, A. L; Gimenes, C. I; Bonatto, A. C; Monteiro, R. A; Souza, E. M; Pedrosa, F. O; Chubatsu, L. S.
  • Araújo, L. M; Universidade Federal do Paraná. Departamento de Bioquímica e Biologia Molecular. Curitiba. BR
  • Huergo, L. F; Universidade Federal do Paraná. Departamento de Bioquímica e Biologia Molecular. Curitiba. BR
  • Invitti, A. L; Universidade Federal do Paraná. Departamento de Bioquímica e Biologia Molecular. Curitiba. BR
  • Gimenes, C. I; Universidade Federal do Paraná. Departamento de Bioquímica e Biologia Molecular. Curitiba. BR
  • Bonatto, A. C; Universidade Federal do Paraná. Departamento de Bioquímica e Biologia Molecular. Curitiba. BR
  • Monteiro, R. A; Universidade Federal do Paraná. Departamento de Bioquímica e Biologia Molecular. Curitiba. BR
  • Souza, E. M; Universidade Federal do Paraná. Departamento de Bioquímica e Biologia Molecular. Curitiba. BR
  • Pedrosa, F. O; Universidade Federal do Paraná. Departamento de Bioquímica e Biologia Molecular. Curitiba. BR
  • Chubatsu, L. S; Universidade Federal do Paraná. Departamento de Bioquímica e Biologia Molecular. Curitiba. BR
Braz. j. med. biol. res ; 41(4): 289-294, Apr. 2008. ilus
Article Dans Anglais | LILACS | ID: lil-479679
ABSTRACT
Azospirillum brasilense is a diazotroph found in association with important agricultural crops. In this organism, the regulation of nitrogen fixation by ammonium ions involves several proteins including the uridylyltransferase/uridylyl-removing enzyme, GlnD, which reversibly uridylylates the two PII proteins, GlnB and GlnZ, in response to the concentration of ammonium ions. In the present study, the uridylylation/deuridylylation cycle of A. brasilense GlnB and GlnZ proteins by GlnD was reconstituted in vitro using the purified proteins. The uridylylation assay was analyzed using non-denaturing polyacrylamide gel electrophoresis and fluorescent protein detection. Our results show that the purified A. brasilense GlnB and GlnZ proteins were uridylylated by the purified A. brasilense GlnD protein in a process dependent on ATP and 2-oxoglutarate. The dependence on ATP for uridylylation was similar for both proteins. On the other hand, at micromolar concentration of 2-oxoglutarate (up to 100 µM), GlnB uridylylation was almost twice that of GlnZ, an effect that was not observed at higher concentrations of 2-oxoglutarate (up to 10 mM). Glutamine inhibited uridylylation and stimulated deuridylylation of both GlnB and GlnZ. However, glutamine seemed to inhibit GlnZ uridylylation more efficiently. Our results suggest that the differences in the uridylylation pattern of GlnB and GlnZ might be important for fine-tuning of the signaling pathway of cellular nitrogen status in A. brasilense.
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Texte intégral: Disponible Indice: LILAS (Amériques) Sujet Principal: Protéines bactériennes / Azospirillum brasilense Limites du sujet: Humains Pays comme sujet: Amérique du Sud / Brésil langue: Anglais Texte intégral: Braz. j. med. biol. res Thème du journal: Biologie / Médicament Année: 2008 Type: Article Pays d'affiliation: Brésil Institution/Pays d'affiliation: Universidade Federal do Paraná/BR

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Texte intégral: Disponible Indice: LILAS (Amériques) Sujet Principal: Protéines bactériennes / Azospirillum brasilense Limites du sujet: Humains Pays comme sujet: Amérique du Sud / Brésil langue: Anglais Texte intégral: Braz. j. med. biol. res Thème du journal: Biologie / Médicament Année: 2008 Type: Article Pays d'affiliation: Brésil Institution/Pays d'affiliation: Universidade Federal do Paraná/BR