The basal turnover of yeast branched-chain amino acid permease Bap2p requires its C-terminal tail.

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 Lett

authors

Omura F,Kodama Y,Ashikari T

doi

10.1111/j.1574-6968.2001.tb09471.x

keywords:

subject

Has Abstract

pub_date

2001-01-15 00:00:00

pages

207-14

issue

2

eissn

0378-1097

issn

1574-6968

pii

S0378-1097(00)00532-2

journal_volume

194

pub_type

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