Asset Details
Do you wish to reserve the book?
The proline-rich antimicrobial peptide Api137 disrupts large ribosomal subunit assembly and induces misfolding
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
The proline-rich antimicrobial peptide Api137 disrupts large ribosomal subunit assembly and induces misfolding
Do you wish to request the book?
The proline-rich antimicrobial peptide Api137 disrupts large ribosomal subunit assembly and induces misfolding
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
The proline-rich antimicrobial peptide Api137 disrupts large ribosomal subunit assembly and induces misfolding
2025
Overview
The proline-rich antimicrobial designer peptide Api137 inhibits protein expression in bacteria by binding simultaneously to the ribosomal polypeptide exit tunnel and the release factor (RF), depleting the cellular RF pool and leading to ribosomal arrest at stop codons. This study investigates the additional effect of Api137 on the assembly of ribosomes using an
Escherichia coli
reporter strain expressing one ribosomal protein per 30S and 50S subunit tagged with mCherry and EGFP, respectively. Separation of cellular extracts derived from cells exposed to Api137 in a sucrose gradient reveals elevated levels of partially assembled and not fully matured precursors of the 50S subunit (pre-50S). High-resolution structures obtained by cryogenic electron microscopy demonstrate that a large proportion of pre-50S states are missing up to five proteins (uL22, bL32, uL29, bL23, and uL16) and have misfolded helices in 23S rRNA domain IV. These data suggest a second mechanism for Api137, wherein it disrupts 50S subunit assembly by inducing the formation of misfolded precursor particles potentially incapable of evolving into active ribosomes, suggesting a bactericidal mechanism.
Proline-rich antimicrobial peptides (PrAMPs) are inhibitors of bacterial protein synthesis. Here, the authors demonstrate that the antimicrobial peptide Api137 can disrupt assembly of the ribosomal 50S subunit by inducing misfolding of its components.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82/58
/ Antimicrobial Peptides - chemistry
/ Antimicrobial Peptides - pharmacology
/ Assembly
/ Codons
/ E coli
/ Escherichia coli - drug effects
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Helices
/ Humanities and Social Sciences
/ Peptides
/ Proline
/ Protein Folding - drug effects
/ Proteins
/ Ribosomal Proteins - metabolism
/ Ribosome Subunits, Large, Bacterial - drug effects
/ Ribosome Subunits, Large, Bacterial - metabolism
/ Ribosome Subunits, Large, Bacterial - ultrastructure
/ RNA
/ rRNA
/ rRNA 23S
/ Science
/ Sucrose
