Api137 Peptide
Not For Human Use, Lab Use Only.
C104H171N37O22
Sequence 3 letters:
undefined
Sequence:
Gu-ONNRPVYIPRPRPPHPRL-OH (Gu = N,N,N’,N’-tetramethylGuanidino and O = L-ornithine)
Cas No. :
Molecular Formula:
C104H171N37O22
Molecular Weight:
2291.40
Description
Api137, a derivative of the insect-produced antimicrobial peptide apidaecin, arrests terminating ribosomes using a unique mechanism of action. Api137 binds to the Escherichia coli ribosome and traps release factor (RF) RF1 or RF2 subsequent to the release of the nascent polypeptide chain. A high-resolution cryo-EM structure of the ribosome complexed with RF1 and Api137 reveals the molecular interactions that lead to RF trapping. Api137-mediated depletion of the cellular pool of free release factors causes the majority of ribosomes to stall at stop codons before polypeptide release, thereby resulting in a global shutdown of translation termination.
Reference
- Florin T, Maracci C, Graf M, et al. An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome. Nat Struct Mol Biol. 2017
- bioRxiv preprint doi: https://doi.org/10.1101/2020.05.17.100735. this version posted May 20, 2020.
- Mardirossian M, Barrière Q, Timchenko T, et al. Fragments of the Nonlytic Proline-Rich Antimicrobial Peptide Bac5 Kill Escherichia coli Cells by Inhibiting Protein Synthesis. Antimicrob Agents Chemother. 2018;62(8):e00534-18. Published 2018 Jul 27. doi:10.1128/AAC.00534-18
- Meydan S, Marks J, Klepacki D, et al. Retapamulin-Assisted Ribosome Profiling Reveals the Alternative Bacterial Proteome. Mol Cell. 2019;74(3):481-493.e6
- Adio S, Sharma H, Senyushkina T, et al. Dynamics of ribosomes and release factors during translation termination in E. coli. Elife. 2018
- Florin T, Maracci C, Graf M, et al. An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome. Nat Struct Mol Biol. 2017;24(9):752-757