Creado por gina_evans0312
hace más de 10 años
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Pregunta | Respuesta |
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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