Amino acid residues before the hydrophobic region which are critical for membrane translocation of the N-terminal domain of synaptotagmin II.
We examined the fine structure of the type I signal-anchor sequence of synaptotagmin II, which has a 60-residue N-terminal domain followed by a hydrophobic region (H-region), focusing on the hinge region between the N-terminal and the H-regions. It was found that the charged or highly polar residues support the translocation of the N-terminal domain through the endoplasmic reticulum membrane at specific positions in the hinge. The residue requirement correlated with the turn propensity scale for transmembranes. It is suggested that a certain conformation, likely helical hairpin, in the hinge is critical for N-terminal domain translocation.
Kida
Y
Y
Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, Japan.
Sakaguchi
M
M
Fukuda
M
M
Mikoshiba
K
K
Mihara
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001224:Aspartic Acid / Q000737:chemistry; D006031:Glycosylation; D007425:Intracellular Membranes / Q000378:metabolism*; D008239:Lysine / Q000737:chemistry; D008969:Molecular Sequence Data; D009154:Mutation; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011392:Proline / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D050861:Synaptotagmin II
D009419:Nerve Tissue Proteins; D050861:Synaptotagmin II; D001224:Aspartic Acid; D011392:Proline; D008239:Lysine