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Very‐long‐chain acyl‐CoA dehydrogenase subunit assembles to the dimer form on mitochondrial inner membrane
Author(s) -
Souri Masayoshi,
Aoyama Toshifumi,
Hoganson George,
Hashimoto Takashi
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00343-3
Subject(s) - dimer , protein subunit , inner mitochondrial membrane , chemistry , inner membrane , translocase of the inner membrane , mitochondrion , chain (unit) , biochemistry , stereochemistry , membrane , mitochondrial membrane transport protein , organic chemistry , physics , gene , astronomy
This paper describes the process of dimer assembly of mitochondrial very‐long‐chain acyl‐CoA dehydrogenase (VLCAD) subunit. Mature VLCAD is a homodimer of a 70‐kDa protein associated with the mitochondrial membrane. Newly synthesized VLCAD was present as a monomer and the major fraction was associated with the mitochondrial inner membrane. The association of VLCAD subunit with the mitochondrial membrane was observed early during dimer formation. In contrast, a VLCAD monomeric mutant S583W, a novel mutation identified from a patient with VLCAD deficiency, did not associate with the mitochondrial membrane after import and the major fraction remained in the mitochondrial matrix. These results suggest that association of VLCAD protein with mitochondrial inner membrane is necessary for dimer assembly and formation of mature VLCAD.