Attachment of Ub to Target Protein


Ubiquitin mechanism for protein targeting
Chinazor Okeke
Flowchart by Chinazor Okeke, updated more than 1 year ago
Chinazor Okeke
Created by Chinazor Okeke over 6 years ago

Resource summary

Flowchart nodes

  • 1. -NH of Lys residue on protein is covalently attached to the COO- terminus of Ub 
  • 2. Another Ub attaches to the Lys 48 -NH of the first Ub
  • 3. Repeat Steps 2 twice until you get four covalently attached Ubs
  • 4 Ub's = the DEATH MARK
  • 1. E1 activates the Ub by adenylating -COO with AMP (hydrolysis of ATP into AMP and PPi)
  • 2. E1 transfers Ub onto its Cys residue to form a high E thioester bond, thereby removing AMP
  • 3. A transthiolation reaction transfers an activated Ub from E1 to E2
  • E2 is now bonded to Ub via a thioester bond
  • 4. E3 recognizes and associates with both the E2-Ub complex and the target protein
  • E1 = Ub activating enzyme
  • E2 = Ub conjugating enzyme
  • 5. E3 catalyzes the transfer of Ub onto amino groups on specific Lys on the target protein
  • 6. W/ E3 still bound to the target protein, repeat steps 1-5 until 3 more Ubs are attached
  • E3 = scaffold b/c it recognizes both target protein and E2-Ub complex
  • E3 = Ub ligating enzyme
  • Ubiquitin Targeting and Mechanism
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