Back

The Pvc15 D2-Pnf SP Interaction Mediates AAA ATPase Activity, Payload Stability, and Translocation into the PVC Tube Lumen.

Waterfield, N. R.; Evans, R.

2023-08-15 microbiology
10.1101/2023.08.15.553202 bioRxiv
Show abstract

The Photorhabdus virulence cassette (PVC) is an elegant, multi-protein, contractile nanostructure which injects functionally bioactive polypeptides into the eukaryotic cytosol. Signal peptides (SPs) are N-terminal amino acid motifs from native payload proteins which can also associate wide range of heterologous proteins to the PVC tube lumen. In addition, Pvc15 is a classic AAA ATPase encoded within the PVC operon which encodes an N-domain and tandem AAA domains D1 and D2. This work finds that Pvc15s ATPase activity is mediated by the E555 residue situated in the Walker B motif of the sole functional ATPase domain, D2. Pvc15 multimerisation may be required to translocate payload into the PVC tube lumen, which is facilitated by intact N and D1 domains. In addition, ATPase activity requires the presence of other PVC operon components which hints at a PVC-regulated mode of action for loading. Furthermore, D2 is a chaperone for the native Pnf SP, though C-terminal truncations of the Pnf SP confers Pvc15-independent stability to the payload. These findings provide insight into the nuanced roles of the Pvc15-SP interaction for payload-PVC association and the effects that SP length and type has on payload stability and PVC-loading ability.

Matching journals

The top 5 journals account for 50% of the predicted probability mass.

50% of probability mass above

"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.