Identifying subunits of ATP synthase TF0·F1 in contact with phospholipid head groups α‐Subunits are labelled selectively by a new photoreactive phospholipid designed for hydrophilic photolabelling

FEBS Letters

Gao, Zhan¹  Bäuerlein, Edmund¹ 

[1] Max-Planck-Institut für Biochemie, Abteilung Membranbiochemie, D-8033 Martinsried, FRG

关键词: ATP synthase;    Photoreactive phospholipid;    Hydrophilic photolabeling;    α-Subunit;    Membrane surface;    (Thermophilic bacterium P53);    ASA-PE 1;    2-dipalmitoyl-sn-glycero-3 phospho-N-(4-azido-2-hydroxybenzoyl)ethanolamine;    125I-ASA-PE 1;    2-dipalmitoyl-sn-glycero-3-phospho-N-(4-azido-3-[1251] iodo-2-hydroxybenzoyl)ethanolamine;    NBD-PE;    N(4-nitro-2;    1;    3-benzoxadiazolyl)phosphati dylethanolamine;   

DOI  :  10.1016/0014-5793(87)80320-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A new phospholipid photolabel was introduced by modifying 1,2-dipalmitoylphosphatidylethanolamine with 4-azidosalicylate to 1,2-dipalmitoyl-sn-glycero-3-phospho-N-(4-azido-2-hydroxybenzoyl)ethanolamine (ASA-PE), which could be radioiodinated easily to ¹²⁵ I-ASA-PE. The ATP synthase TF₀·F₁ of the thermophilic bacterium PS3 was reconstituted with soybean phospholipids forming proteoliposomes with high ATP-³² P_i exchange activity. These proteoliposomes were incubated with ₁₂₅I-ASA-PE to provide its selective incorporation into the outside of the phospholipid bilayer. Upon illumination with ultraviolet light α-subunits of TF₁ were predominantly labelled.

【 授权许可】

Unknown