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The mitochondrial inner membrane AAA metalloprotease family in metazoans
Author(s) -
Juhola M.Katariina,
Shah Zahid H.,
Grivell Leslie A.,
Jacobs Howard T.
Publication year - 2000
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(00)01989-x
Subject(s) - drosophila melanogaster , caenorhabditis elegans , biology , saccharomyces cerevisiae , metalloproteinase , inner membrane , mutant , genetics , aaa proteins , basigin , mitochondrion , gene , yeast , microbiology and biotechnology , model organism , mutation , matrix metalloproteinase , biochemistry , enzyme , atpase
Three metalloproteases belonging to the AAA superfamily (Yme1p, Afg3p and Rca1p) are involved in protein turnover and respiratory chain complex assembly in the yeast inner mitochondrial membrane. Analysis of the completed genome sequences of Caenorhabditis elegans and Drosophila melanogaster indicates that this gene family typically comprises 3–4 members in metazoans. Phylogenetic analysis reveals three main branches represented, respectively, by Saccharomyces cerevisiae YME1 , human SPG7 (paraplegin) and S. cerevisiae AFG3 and RCA1 . mt‐AAA metalloproteases are weak candidates for several previously studied Drosophila mutants. A full elucidation of the cellular and physiological roles of mt‐AAA metalloproteases in metazoans will require the creation of targeted mutations.