Isolation and characterization of a mutant of Neurospora crassa deficient in general amino acid permease activity.
A mutant of Neurospora crassa (pm-nbg27) was isolated on the basis of its resistance of p-fluoro-phenylalanine on ammonium-deficient Vogel's medium. This mutant was found to be devoid of both conidial and post-conidial (after 180 min of preincubation) transport activity of all amino acids. Genetic analysis of pm-nbg27 by crossing it to wild-type (74A) resulted in the predicted segregants exhibiting transport characteristics of pm-n, pm-b, pm-g, pm-nb, pm-ng, pm-bg and parental types. The above observations confirm the postulated general amino acid permease system as well as a single genetic locus control of that activity.
D001120:Arginine / Q000378:metabolism*; D005796:Genes; D005827:Genetics, Microbial; D026901:Membrane Transport Proteins / Q000378:metabolism*; D009154:Mutation; D009491:Neurospora / Q000378:metabolism*; D009492:Neurospora crassa / Q000302:isolation & purification / Q000378:metabolism*; D010649:Phenylalanine / Q000378:metabolism*; D010135:p-Fluorophenylalanine / Q000378:metabolism
D026901:Membrane Transport Proteins; D010649:Phenylalanine; D010135:p-Fluorophenylalanine; D001120:Arginine