Mitochondrial small subunit ribosome proteomics
downstream-application
Bovine mitochondrial small subunit ribosomal proteins resolved by two-dimensional PAGE, in-gel tryptic digestion, capillary LC and electrospray MS/MS, with the resulting peptide sequences used as virtual probes to screen the human EST database by tBLASTN and assemble consensus cDNAs in silico. Spectra without an exact match in either the protein or EST databases were sequenced de novo, manually or with PepSeq. Seven proteins are reported in Table I, and the two de novo-derived peptides are the sole identifying evidence for two of them, MRP-S26 and MRP-S14; MRP-S14 is also one of only two proteins in the study with significant prokaryotic homology, to Escherichia coli S14. Five of the seven belong to a new class of ribosomal proteins with no prokaryotic counterpart.
| Kind | downstream-application |
| Deep learning | no |
| Acquisition | DDA |
| Application area | general-proteomics |
Papers
- A Proteomics Approach to the Identification of Mammalian Mitochondrial Small Subunit Ribosomal Proteins (2000, Journal of Biological Chemistry, peer-reviewed)