A leucine motif in the amino acid sequence of subunit 9 of the mitochondrial ATPase, and other hydrophobic membrane proteins, that is highly conserved by editing

FEBS Letters

Møller, Ian M.¹  Konstantinov, Yuri M.² 

[1] Department of Plant Biology, Lund University, Box 117, S-221 00 Lund,Sweden;Laboratory of Plant Genetic Engineering, Siberian Institute of Plant Physiology and Biochemistry, PO Box 1243, Irkutsk 664033, Russian Federation

关键词: Amino acid sequence analysis;    F0F1-ATPase;    Helix-helix interaction;    Mitochondrion;    Quaternary protein structure;    RNA editing;   

DOI  :  10.1016/0014-5793(94)01124-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Subunit 9 of the mitochondrial ATPase, but also other hydrophobic mitochondrially encoded proteins, contains a high frequency of the leucine motif, -Leu-X₉-Leu-, which is highly conserved through RNA editing. The leucine motif may provide specific recognition sites between membrane-spanning domains of the F₀-ATPase and between other hydrophobic subunits during the assembly of multienzyme complexes in the inner mitochondrial membrane.

【 授权许可】

Unknown