Amino acid residues before the hydrophobic region which are critical for membrane translocation of the N‐terminal domain of synaptotagmin II

FEBS Letters

Kida, Yuichiro²  Mihara, Katsuyoshi²  Fukuda, Mitsunori¹  Mikoshiba, Katsuhiko¹  Sakaguchi, Masao² 

[1] Laboratory for Developmental Neurobiology, Brain Science Institute, RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan;Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan

关键词: Membrane topology;    Signal sequence;    Membrane protein;    Membrane integration;    Synaptotagmin;    ER;    endoplasmic reticulum;    N-domain;    amino-terminal domain;    H-region;    hydrophobic region;    RM;    rough microsomal membranes;    SA-I;    type I signal anchor;    Syt II;    synaptotagmin II;    SRP;    signal recognition particle;   

DOI  :  10.1016/S0014-5793(01)03000-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown