The basal turnover of yeast branched-chain amino acid permease Bap2p requires its C-terminal tail.
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.
Omura
F
F
Institute for Fundamental Research, Suntory Ltd., 1-1-1, Wakayamadai, Shimamoto-cho, Mishima-gun, 618-8503, Osaka, Japan. fumihiko_omura@suntory.co.jp
Kodama
Y
Y
Ashikari
T
T
D026905:Amino Acid Transport Systems; D019084:Fluorescent Antibody Technique, Indirect; D017353:Gene Deletion; D049452:Green Fluorescent Proteins; D006207:Half-Life; D008164:Luminescent Proteins / Q000235:genetics / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins
D026905:Amino Acid Transport Systems; C097094:BAP2 protein, S cerevisiae; D008164:Luminescent Proteins; D026901:Membrane Transport Proteins; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; D049452:Green Fluorescent Proteins