Trans-membrane translocation of a myristylated protein amino terminus.
Hepatitis B virus surface protein variants are described, capable of translocating to the lumenal side of the endoplasmic reticulum membrane their myristylated N-termini, as revealed by the contestual modification of N-terminal, N-linked glycosylation sites. To our knowledge, this is the first example of transmembrane translocation of a preformed protein acyl adduct. The possible significance of this event for hepatitis B virus biology is discussed.
Gallina
A
A
Istituto di Genetica Biochimica ed Evoluzionistica, Consiglio Nazionale delle Ricerche, Pavia, Italy.
Milanesi
G
G
D000595:Amino Acid Sequence; D001483:Base Sequence; D002460:Cell Line; D003062:Codon / Q000235:genetics; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006514:Hepatitis B Surface Antigens / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D006515:Hepatitis B virus / Q000378:metabolism; D006801:Humans; D007425:Intracellular Membranes / Q000378:metabolism; D008051:Lipid Bilayers / Q000378:metabolism; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D019814:Myristic Acid; D009227:Myristic Acids / Q000378:metabolism*; D009838:Oligodeoxyribonucleotides; D010957:Plasmids
D003062:Codon; D006514:Hepatitis B Surface Antigens; D008051:Lipid Bilayers; D009227:Myristic Acids; D009838:Oligodeoxyribonucleotides; D019814:Myristic Acid