TABLE 2.
Relative abundance of posttranslational modifications to mitochondrial proteins in hamster prion-infected Tg7 mice
| Protein name | Protein identifier | PTMa | Fold Δb | P valuec |
|---|---|---|---|---|
| 28S ribosomal protein S34 | Q9JIK9 | Deamidation (NQ) | 24.9 | 0.002 |
| NADH dehydrogenase 1 α subcomplex subunit 9 | Q9DC69 | Pyro-glu from Q | 5.0 | 0.02 |
| Isoleucyl-tRNA synthetase | Q8BIJ6 | Pyro-glu from Q | 4.1 | 0.02 |
| Sideroflexin-1 | Q99JR1 | Acetylation (N-term) | 2.1 | 0.01 |
| Voltage-dependent anion-selective channel protein 2 | Q60930 | Acetylation (N-term) | 1.7 | 0.003 |
| Mitochondrial inner membrane protein | Q8CAQ8 | Pyro-glu from Q | 1.7 | 0.01 |
| Cytochrome b-c1 complex subunit 2 | Q9DB77 | Deamidation (NQ) | −1.3 | 0.003 |
| Sideroflexin 1 | Q99JR1 | Oxidation (M) | −1.3 | 0.03 |
| NADH dehydrogenase 1 α subcomplex subunit 12 | Q7TMF3 | Acetylation (N-term) | −1.4 | 0.003 |
| Glutamate dehydrogenase 1 | P26443 | Deamidation (NQ) | −1.6 | 0.005 |
| Cytochrome c1 heme protein | Q9D0M3 | Deamidation (NQ) | −1.6 | 0.02 |
| ATP synthase subunit α | Q03265 | Deamidation (NQ) | −1.8 | 0.03 |
| NADH dehydrogenase iron-sulfur protein 3 | Q9DCT2 | Pyro-glu from Q | −1.9 | 0.005 |
| Ca2+-binding mitochondrial carrier protein Aralar1 | Q8BH59 | Deamidation (NQ) | −1.9 | 0.04 |
| ATP synthase subunit α | Q03265 | Sodium adduct | −2.2 | 0.03 |
| Ca2+-binding mitochondrial carrier protein Aralar1 | Q8BH59 | Deamidation (NQ) | −2.4 | 0.03 |
| ATP synthase subunit α | Q03265 | Formylation | −2.4 | 0.003 |
| NADH dehydrogenase iron-sulfur protein 2 | Q91WD5 | Oxidation (M) | −2.5 | 0.01 |
| Mitochondrial inner membrane protein | Q8CAQ8 | Pyro-glu from Q | −2.7 | 0.03 |
| Cytochrome c oxidase subunit 4 isoform 1 | P19783 | Deamidation (NQ) | −3.3 | 0.04 |
Posttranslational modification (PTM) identified on a single peptide from the protein identified. The amino acids altered are indicated. A protein occurring multiple times in the list indicates that more than one peptide with a PTM was identified. SpCs were derived using the PEAKS Studio version 8 software package. M, methionine; Q, glutamine; NQ, asparagine and glutamine; N-term, N-terminal amino group of peptide.
Fold change was calculated from the average normalized SpC values from each group and indicates the change in relative abundance in Tg7Sc mice from that in Tg7NBH mice. If either group had an average SpC of 0, the value of 1 was assigned to obtain an accurate fold change.
P values were calculated using the Student t test to compare SpC in Tg7NBH mice to SpC in Tg7Sc mice.