Abstract:
: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.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Omura F,Kodama Y,Ashikari Tdoi
10.1111/j.1574-6968.2001.tb09471.xkeywords:
subject
Has Abstractpub_date
2001-01-15 00:00:00pages
207-14issue
2eissn
0378-1097issn
1574-6968pii
S0378-1097(00)00532-2journal_volume
194pub_type
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