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Título : Role of GOGAT in carbon and nitrogen partitioning in Rhizobium etli
Creador: Castillo, A
Nivel de acceso: Open access
Palabras clave : Secuencia de aminoácidos - Datos de Secuencia Molecular
Carbon - metabolismo
glutamato sintasa - genética
glutamato sintasa - metabolismo
Ácido glutámico - metabolismo
Mutagénesis Insercional - genética
Nitrógeno - Metabolismo
Compuestos de Amonio Cuaternario - metabolismo
Rhizobium -enzimología
Rhizobium - genética
Rhizobium - crecimiento y desarrollo
Alineación de Secuencia - instrumentación
Ácido Succínico - metabolismo
Amino Acid Sequence - Molecular Sequence Data
Carbon - metabolism
Glutamate Synthase -genetics
Glutamate Synthase -metabolism
Glutamic Acid -metabolism
Mutagenesis, Insertional - genetics;
Nitrogen - metabolism
Quaternary Ammonium Compounds -metabolism
Rhizobium - enzymology
Rhizobium- genetics Rhizobium - growth & development
Sequence Alignment - instrumentation
Succinic Acid -metabolism
asimilación de nitrógeno
metabolismo del carbono
rotación de la glutamina
nitrógeno
fijación
auxotroph glutamato
nitrogen assimilation
carbon metabolism
glutamine turnover
nitrogen
fixation
glutamate auxotroph
Descripción : The isolation and characterization of a Rhizobium etli glutamate auxotroph, TAD12, harbouring a single Tn5 insertion, is reported. This mutant produced no detectable glutamate synthase (GOGAT) activity. The cloning and physical characterization of a 7<2 kb fragment of R. etli DNA harbouring the structural genes gltB and gltD encoding the two GOGAT subunits GltB and GltD is also reported. In comparison with the wild-type strain (CFN42), the GOGAT mutant strain utilized less succinate and glutamate and grew less with this and other amino acids as nitrogen source. R. etli assimilates ammonium by the glutamine synthetase (GS)-GOGAT pathway and a GOGAT mutant prevents the cycling of glutamine by this pathway, something that impairs nitrogen and carbon metabolism and explains the decrease in the amino-nitrogen during exponential growth, with glutamate as nitrogen source. GOGAT activity also has a role in ammonium turnover and in the synthesis of amino acids and proteins, processes that are necessary to sustain cell viability in non-growing conditions. The assimilation of ammonium is important during symbiosis and glutamate constitutes 20–40% of the total amino-nitrogen. In symbiosis, the blockage of ammonium assimilation by a GOGAT mutation significantly decreases the amino-nitrogen pool of the bacteroids and may explain why more N2 is fixed in ammonium,
Colaborador(es) u otros Autores: Taboada H
Mendoza A
Valderrama B
Encarnación S
Mora J.
Fecha de publicación : 2000
Tipo de publicación: Artículo
Formato: pdf
Identificador del Recurso : 10.1099/00221287-146-7-1627
Fuente: Microbiology 146(7):1627-37
URI : http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2778
Idioma: eng
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