Abstract
Initiation factor 3 (IF3) is a conserved translation factor. Mutations in mitochondrial IF3 (IF3mt) have been implicated in disease pathology. Escherichia coli infCΔ55, compromised for IF3 activity, has provided an excellent heterologous system for IF3mt structure-function analysis. IF3mt allowed promiscuous initiation from AUA, AUU and ACG codons but avoided initiation with initiator tRNAs lacking the conserved 3GC pairs in their anticodon stems. Expression of IF3mt N-terminal domain, or IF3mt devoid of its typical N-, and C-terminal extensions improved fidelity of initiation in E. coli. The observations suggest that the IF3mt terminal extensions relax the fidelity of translational initiation in mitochondria.
Original language | English (US) |
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Pages (from-to) | 1-8 |
Number of pages | 8 |
Journal | Mitochondrion |
Volume | 39 |
DOIs | |
State | Published - Mar 2018 |
Externally published | Yes |
Keywords
- Fidelity
- Initiation factor 3
- Mitochondria
- Protein synthesis
- Ribosome
ASJC Scopus subject areas
- Molecular Medicine
- Molecular Biology
- Cell Biology