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http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2778
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: | |
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 |
Aparece en las colecciones: | Artículos |
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