Effect of aniA (carbon flux regulator) and PhaC (poly-beta-hydroxybutyrate synthase) mutations on pyruvate metabolism in Rhizobium etli.
The Rhizobium etli poly-beta-hydroxybutyrate synthase (PhaC) mutant SAM100 grows poorly with pyruvate as the carbon source. The inactivation of aniA, encoding a global carbon flux regulator, in SAM100 restores growth of the resulting double mutant (VEM58) on pyruvate. Pyruvate carboxylase (PYC) activity, pyc gene transcription, and holoenzyme content, which were low in SAM100, were restored in strain VEM58. The genetically engineered overexpression of PYC in SAM100 also allowed its growth on pyruvate. The possible relation between AniA, pyc transcription, and reduced-nucleotide levels is discussed.
Dunn
Michael F
MF
Programa de Ingeniería Metabólica, Centro de Investigación sobre Fijación de Nitrógeno, Universidad Nacional Autónoma de México, Cuernavaca, Morelos, Mexico. mike@cifn.unam.mx
Araíza
Gisela
G
Encarnación
Sergio
S
del Carmen Vargas
María
M
Mora
Jaime
J
D000217:Acyltransferases / Q000502:physiology*; D000942:Antigens, Bacterial / Q000502:physiology*; D001425:Bacterial Outer Membrane Proteins / Q000502:physiology*; D002952:Citric Acid Cycle; D009154:Mutation; D011766:Pyruvate Carboxylase / Q000235:genetics / Q000378:metabolism; D019289:Pyruvic Acid / Q000378:metabolism*; D012231:Rhizobium / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic
D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; C077531:aniA protein, Neisseria gonorrhoeae; D019289:Pyruvic Acid; D000217:Acyltransferases; C060970:poly-beta-hydroxybutyrate polymerase; D011766:Pyruvate Carboxylase