Open AccessThe basal turnover of yeast branched‐chain amino acid permease Bap2p requires its C‐terminal tail
Author(s) -
Omura Fumihiko,
Kodama Yukiko,
Ashikari Toshihiko
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb09471.x
Subject(s) - permease , biochemistry , valine , saccharomyces cerevisiae , leucine , amino acid , yeast , isoleucine , chemistry , protein turnover , green fluorescent protein , biology , transporter , microbiology and biotechnology , protein biosynthesis , gene
The branched‐chain amino acid permease Bap2p is a transport system for leucine, isoleucine, and valine in Saccharomyces cerevisiae , and its synthesis is regulated transcriptionally. However, the downregulation mechanisms of Bap2p have not been established. Here we demonstrate that the C‐terminal region of Bap2p plays a pivotal role in its basal turnover. Truncation of the C‐terminal 29 residues caused the stabilization and accumulation in the plasma membrane of Bap2p. Furthermore, when the Bap2p C‐terminal region was fused to green fluorescent protein, the fusion protein localized to the plasma membrane, suggesting the existence of a possible degradation‐related acceptor site for the C‐terminal tail of Bap2p.