Mutations in Neurospora crassa which affect multiple amino acid transport systems.
Biochim Biophys Acta, 1976/7/15;436(4):774-88.
PMID: 133719
Abstract
Characterization of a double mutant, his-6: hgu-4, which is unable to utilize L-histidyl-glycine as a source of histidine has revealed a new locus on linkage group V. The hgu-4 genotype results in a generalized reduced transport activity for amino acids, with a concomitant increased resistance to amino acid analogs. Transport rates and analog resistance for amino acids by this mutant are compared to the previously reported transport deficient mutants fpr-1, nap and un-3. Transport of L-aspartate as a function of temperature is examined in a variety of transport deficient strains in an attempt to explain the mode of action of mutation which pleiotropically affect several genetically and biochemically distinct amino acid transport systems.
MeSH terms
Amino Acids; Arginine; Aspartic Acid; Biological Transport, Active; Cell Division; Chromosome Mapping; Kinetics; Mutation; Neurospora; Neurospora crassa; Phenylalanine; Structure-Activity Relationship
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