769691
Descrição
FlashCards por gina_evans0312, atualizado more than 1 year ago
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Criado por gina_evans0312
aproximadamente 10 anos atrás
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| Questão | Responda |
| 20S Subunit- Structure | 4 subunits (alternating 2 alpha, 2 beta) with a and b going opposite ways |
| 20S Subunit- Protease | Non specific protease sequestered in the middle, only accessed via a narrow channel |
| 20S Subunit- Protein Unfolding | Proteins must be unfolded to pass through the channel to the protease, so fully folded proteins are protected from accidents |
| 20S Subunit- Protein Selection | Only ubiquitinated proteins are brought to the proteosome |
| 19s Lid- Role | Acts as adocking site, with ATPases and unfoldases to unfold the target protein |
| Ubiquitin | A 76 aa polypeptide used to flag amino acids for degredation |
| Ubiquitination- E1 | Ubiquitin activating enzyme |
| Ubiquitination- E1 Role | Ubi binds to it before transfer to E2 |
| Ubiquitination- E2 | Ubiquitin Conjugating Enzyme |
| Ubiquitination- E2 Role | Transfers E2 to E3 |
| Ubiquitination- E3 | Ubiquitin Ligating Enzyme |
| Ubiquitination- E3 Role | Transers ubi to the lysine residue of the target protein |
| Ubiquitination- Polyubiquitination | If degredation is the aim, the process repeats, adding multiple Ubis together |
| Ubiquitination- Recycling | Ubis are removed from broken down proteins and reused |
| Ubiquitination- Cell Growth | Regulates cell growth & proliferation by degrading uncessary transcription factors |
| Ubiquitination- Mistakes | Removes misfolded/mistargeted proteins |
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