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The mature AEP2 gene product of Saccharomyces cerevisiae , required for the expression of subunit 9 of ATP synthase, is a 58 kDa mitochondrial protein
Author(s) -
Patrick M. Finnegan,
Ellis Tp,
Phillip Nagley,
Lukins Hb
Publication year - 1995
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(95)00727-q
Subject(s) - complementation , gene product , protein subunit , gene , saccharomyces cerevisiae , biology , atp synthase , biochemistry , microbiology and biotechnology , mitochondrion , scn3a , hspa9 , nucleic acid sequence , peptide sequence , nuclear gene , gene expression , mitochondrial dna , g alpha subunit , phenotype
The nucleotide sequence of the yeast nuclear AEP2 gene, required for the expression of the mitochondrial DNA–encoded subunit 9 of ATP synthase, predicts a primary translation product of 67.5 kDa. The ATP13 gene is allelic to AEP2 but was reported to encode a protein of about 42 kDa in size. We thus investigated genetically and biochemically the size of the AEP2 gene product. Genetic complementation assays using 3′ truncated AEP2 genes, here shows that function is abolished by the removal of only 32 amino acids from the C–terminus of the predicted protein product. Cell–free translation of AEP2 produces a 64 kDa polypeptide (consistent with the AEP2 sequence) which is imported into mitochondria and processed to a 58 kDa product by the removal of a presequence of about 50 amino acids.