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Identification of MIM23, a putative component of the protein import machinery of the mitochondrial inner membrane
Author(s) -
Dekker Peter J.T.,
Keil Petra,
Rassow Joachim,
Maarse Ammy C.,
Pfanner Nikolaus,
Meijer Michiel
Publication year - 1993
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 - 10.1016/0014-5793(93)80921-g
Subject(s) - translocase of the inner membrane , inner membrane , inner mitochondrial membrane , complementation , mitochondrial carrier , vesicle associated membrane protein 8 , mutant , atp–adp translocase , membrane protein , biology , mitochondrion , mitochondrial membrane transport protein , microbiology and biotechnology , transport protein , biochemistry , gene , bacterial outer membrane , membrane , escherichia coli
A screening for yeast mutants impaired in mitochondrial protein import led to the identification of two genes ( MPI1 and MPI2 ) encoding the essential components MIM44 and MIM17 of the inner membrane import machinery. We analyzed twelve additional mutants obtained in the screening and found two further complementation groups. One group represents mutants of SSC1 , the gene encoding mitochondrial hsp70, an essential matrix protein required for protein import across the inner membrane. The second complementation group represents mutants of a new gene ( MPI3 ) encoding a 23 kDa integral inner membrane protein (MIM23). MIM23 is synthesized without a presequence, and its import to the inner membrane requires a membrane potential. MIM23 contains a domain homologous to half of MIM17. We speculate that MIM23 is a new member of the protein import machinery of the mitochondrial inner membrane.