Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2022 Nov 29;50(21):12039–12057. doi: 10.1093/nar/gkac1121

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

PMC Copyright notice

Figure 5. — Model of competitive binding of APOBECs and RPA. The tight binding of RPA on ssDNA acts as a roadblock, limiting APOBECs from catalyzing processive deaminations. (Top panel) This effectively prevents competitive exchange of RPA with APOBECs that can only slide along the DNA backbone, leading to lowered APOBEC specific activity. (Bottom panel) Bound RPA can undergo exchange with free RPA through facilitated dissociation allowing an opportunity for APOBECs to bind. Three-dimensional rapid cycling on/off ssDNA enables APOBECs to compete with RPA for ssDNA as both proteins exchange between bound and free states. The displacement of RPA enables deamination activity from A3s that do not require processive sliding, but instead locate cytosines by cycling on/off the ssDNA.