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A new face on apoptosis: death‐associated protein 3 and PDCD9 are mitochondrial ribosomal proteins
Author(s) -
Koc Emine Cavdar,
Ranasinghe Asoka,
Burkhart William,
Blackburn Kevin,
Koc Hasan,
Moseley Arthur,
Spremulli Linda L.
Publication year - 2001
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(01)02250-5
Subject(s) - mitochondrial ribosome , ribosome , ribosomal protein , microbiology and biotechnology , biology , mitochondrion , ribosomal rna , biochemistry , dnaja3 , chemistry , mitochondrial dna , mitochondrial fusion , rna , gene
Two proteins known to be involved in promoting apoptosis in mammalian cells have been identified as components of the mammalian mitochondrial ribosome. Proteolytic digestion of whole mitochondrial ribosomal subunits followed by analysis of the peptides present using liquid chromatography–tandem mass spectrometry revealed that the proapoptotic proteins, death‐associated protein 3 (DAP3) and the programmed cell death protein 9, are both components of the mitochondrial ribosome. DAP3 has motifs characteristic of guanine nucleotide binding proteins and is probably the protein that accounts for the nucleotide binding activity of mammalian mitochondrial ribosomes. The observations reported here implicate mitochondrial protein synthesis as a major component in cellular apoptotic signaling pathways.