A new face on apoptosis: death-associated protein 3 and PDCD9 are mitochondrial ribosomal proteins.
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.
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Related Subject Headings
- Sequence Homology, Amino Acid
- Ribosomal Proteins
- RNA-Binding Proteins
- Proteins
- Protein Prenylation
- Molecular Sequence Data
- Mitochondria
- Mass Spectrometry
- In Vitro Techniques
- Humans
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Sequence Homology, Amino Acid
- Ribosomal Proteins
- RNA-Binding Proteins
- Proteins
- Protein Prenylation
- Molecular Sequence Data
- Mitochondria
- Mass Spectrometry
- In Vitro Techniques
- Humans