AP profiling resolves co-translational folding pathway and chaperone interactions in vivo
Chen, X.; Kaiser, C.
Show abstract
Natural proteins have evolved to fold robustly along specific pathways. Folding begins during synthesis, guided by interactions of the nascent protein with the ribosome and molecular chaperones. However, the timing and progression of co-translational folding remain largely elusive, in part because the process is difficult to measure in the natural environment of the cytosol. We developed a high-throughput method to quantify co-translational folding in live cells that we term Arrest Peptide profiling (AP profiling). We employed AP profiling to delineate co-translational folding for a set of GTPase domains with very similar structures, defining how topology shapes folding pathways. Genetic ablation of major nascent chain-binding chaperones resulted in localized folding changes that suggest how functional redundancies among chaperones are achieved by distinct interactions with the nascent protein. Collectively, our studies provide a window into cellular folding pathways of complex proteins and pave the way for systematic studies on nascent protein folding at unprecedented resolution and throughput.
Matching journals
The top 3 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria 96%
- Conserved heterodimeric GTPase Rbg1/Tma46 promotes efficient translation in eukaryotic cells 96%
- Polysomes and mRNA control the biophysical properties of the eukaryotic cytoplasm 95%
Similar papers in this journal
- The phage protein paratox is a multifunctional metabolic regulator of Streptococcus 96%
- Dynamic ParB-DNA interactions initiate and maintain a partition condensate for bacterial chromosome segregation 96%
- The transitional kinetics between open and closed Rep structures can be tuned by salt via two intermediate states 95%
Similar papers in this journal
- Filament formation activates protease and ring nuclease activities of CRISPR SAVED-Lon 96%
- Mechanism of chaperone coordination during cotranslational protein folding in bacteria 96%
- RAPIDASH: A tag-free enrichment of ribosome-associated proteins reveals compositional dynamics in embryonic tissues and stimulated macrophages 96%
Similar papers in this journal
- Dynamic interactions between the RNA chaperone Hfq, small regulatory RNAs and mRNAs in live bacterial cells 96%
- Coil-to-Helix Transition at the Nup358-BicD2 Interface Activates BicD2 for Dynein Recruitment 96%
- Staphylococcus aureus FtsZ and PBP4 bind to the conformationally dynamic N-terminal domain of GpsB 96%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.