| Autor: |
Kuppa, Sahiti, Deveryshetty, Jaigeeth, Chadda, Rahul, Mattice, Jenna R., Pokhrel, Nilisha, Kaushik, Vikas, Patterson, Angela, Dhingra, Nalini, Pangeni, Sushil, Sadauskas, Marisa K., Shiekh, Sajad, Balci, Hamza, Ha, Taekjip, Zhao, Xiaolan, Bothner, Brian, Antony, Edwin |
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| Zdroj: |
Nature Communications; 9/2/2022, Vol. 13 Issue 1, p1-16, 16p |
| Abstrakt: |
Replication Protein A (RPA) is a heterotrimeric complex that binds to single-stranded DNA (ssDNA) and recruits over three dozen RPA-interacting proteins to coordinate multiple aspects of DNA metabolism including DNA replication, repair, and recombination. Rtt105 is a molecular chaperone that regulates nuclear localization of RPA. Here, we show that Rtt105 binds to multiple DNA binding and protein-interaction domains of RPA and configurationally staples the complex. In the absence of ssDNA, Rtt105 inhibits RPA binding to Rad52, thus preventing spurious binding to RPA-interacting proteins. When ssDNA is available, Rtt105 promotes formation of high-density RPA nucleoprotein filaments and dissociates during this process. Free Rtt105 further stabilizes the RPA-ssDNA filaments by inhibiting the facilitated exchange activity of RPA. Collectively, our data suggest that Rtt105 sequesters free RPA in the nucleus to prevent untimely binding to RPA-interacting proteins, while stabilizing RPA-ssDNA filaments at DNA lesion sites. The single stranded DNA binding protein RPA coordinates DNA metabolism using multiple protein and DNA interaction domains. Here, the authors show that the chaperone-like protein Rtt105 staples RPA domains to prevent untimely protein interactions. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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