Cloning and characterization of an aromatic amino acid and leucine permease of Penicillium chrysogenum.

نویسندگان

  • Hein Trip
  • Melchior E Evers
  • Wil N Konings
  • Arnold J M Driessen
چکیده

The gene encoding the amino acid permease ArlP (Aromatic and leucine Permease) was isolated from the filamentous fungus Penicillium chrysogenum after PCR using degenerated oligonucleotides based on conserved regions of fungal amino acid permeases. The cDNA clone was used for expression of the permease in Saccharomyces cerevisiae M4054, which is defective in the general amino acid permease Gap1. Upon overexpression, an increase in the uptake of L-tyrosine, L-phenylalanine, L-tryptophan and L-leucine was observed. Further competition experiments indicate that ArlP recognizes neutral and aromatic amino acids with an unbranched beta-carbon atom.

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PcMtr, an aromatic and neutral aliphatic amino acid permease of Penicillium chrysogenum.

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عنوان ژورنال:
  • Biochimica et biophysica acta

دوره 1565 1  شماره 

صفحات  -

تاریخ انتشار 2002