The mitochondrial ATP synthase inhibitor protein binds near the C‐terminus of the F1 β‐subunit

FEBS Letters

Jackson, Philip J.¹  Harris, David A.¹ 

[1] Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, England

关键词: Mitochondria;    ATP synthase;    F1 -ATPase;    ATPase inhibitor protein;    (Bovine heart);    EEDQ;    N-ethoxycarbonyl-2-ethoxy-1;    2-dihydroquinoline;    HPLC;    high-performance liquid chromatography;    IF1;    mitochondrial ATP synthase inhibitor protein;    PTH;    phenylthiohydantoin;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(88)80832-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The specific, mitochondrial ATP synthase protein (IF₁) was covalently cross-linked to its binding site on the catalytic sector of the enzyme (F₁-ATPase). The cross-linked complex was selectively cleaved, leaving IF₁ intact to facilitate the subsequent purification of the F₁ fragment to which IF₁ was cross-linked. This fragment was identified by sequence analysis as comprising residues 394–459 on the F₁ β-subunit, near the C-terminus. This finding is discussed in the light of secondary structure predictions for both IF₁ and the F₁ β-subunit, and sequence homologies between mitochondrial and other ATP synthases.

【 授权许可】

Unknown