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The Branched‐Chain Amino Acid Permease Gene of Saccharomyces cerevisiae , BAP2 , Encodes the High‐Affinity Leucine Permease (S1)
Author(s) -
SCHREVE JAMES,
GARRETT JINNIE M.
Publication year - 1997
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/(sici)1097-0061(199704)13:5<435::aid-yea95>3.0.co;2-t
Subject(s) - permease , biology , leucine , gene , biochemistry , lactose permease , amino acid , chain (unit) , genetics , transporter , physics , astronomy
The amino acid leucine has been shown previously to be transported into a yeast cell by at least three permeases: the general amino acid permease, a high‐affinity permease (S1) and a low‐affinity permease (S2). We isolated the gene BAP2 as a multicopy suppressor of the YPD − phenotype of aat1leu2 yeast. BAP2 has been identified previously as encoding an amino acid permease which transports branched‐chain amino acids. In order to align the genetic and biochemical studies of leucine uptake we completed a detailed kinetic analysis of yeast strains in which the BAP2 gene was disrupted and compared this to the kinetics of uptake of the parental strain. We demonstrate that BAP2 encodes the high‐affinity leucine permease previously called S1. © 1997 John Wiley & Sons, Ltd.