Translation Elongation Flashcards
What are the steps of translation elongation?
1) Entry of aminoacyl-tRNA
2) Peptide bond formation and transfer
3) Translocation
During elongation, what are the elements in the SSU?
• In the SSU: anticodons of current and incoming tRNA
During elongation, what are the elements in the LSU?
• In the LSU: growing peptide and AA of tRNA
What is translocation?
release of uncharged tRNA (which is in the P site)
Where do the AA-tRNA enter?
Into the empty A site
Describe briefly the amino acid transfer.
From P site to A site (the peptide attaches to the new AA on tRNA)
o Peptide now in the A site then moves to the P site
What factors are involved in the entry of AA-tRNA?
EF-Tu and EF-Ts
What are the roles/activity of EF-Tu?
o Has GTPase activity (it binds GTP)
o Exists in 2 states
Ef-Tu(GTP): activated (bound to GTP)
Ef-Tu(GDP): inactivated (bound to GDP)
o The binding site of the activated EF-Tu is adjacent to the A site
Facilitates the docking of AA-tRNA into the correct position on the ribosome
o The inactive EF-Tu is released
The energy released activates the AA-tRNA to form a peptide bond
What are the roles/activity of EF-Ts?
o Facilitates the binding of GTP on Ef-Tu
o Reactivates Ef-Tu to recycle it
Describe the peptide bond formation and transfer.
• Activated *NH3 is an active nucleophile
• It attacks the C=O of the growing peptide
• The growing peptide thus transfers from P to A
o The peptide attaches to the new AA on tRNA
What is the point of translocation?
• During translocation, the ribosome is moved 3 nucleotides forward from 5’ to 3’ (to the next codon)
o The deacylated (empty) tRNA is released
What are the steps in translocation?
1) LSU “tilts” forward, creating 2 hybrid sites
LSU E / SSU P : contains the deacylated tRNA
LSU P / SSU A : contains the peptidyl tRNA
2) SSU tilts forward
Intact E: contains deacylated tRNA (which will be expelled)
Intact P: P-tRNA
Intact A: empty
What factors are involved in translocation?
EF-G
What is the role of EF-G in translocation?
o EF-G
Exists in 2 states
• EF-G (GTP) : activated
• EF-G (GDP) : inactivated
Binds the same site as EF-Tu (adjacent to A site)
Causes conformational change (hybrid movement)