scholarly journals Replication protein A subunit 3 and the iron efficiency response in soybean

2013 ◽  
Vol 37 (1) ◽  
pp. 213-234 ◽  
Author(s):  
SARAH E. ATWOOD ◽  
JAMIE A. O'ROURKE ◽  
GREGORY A. PEIFFER ◽  
TENGFEI YIN ◽  
MAHBUBUL MAJUMDER ◽  
...  
Keyword(s):  
Protein A ◽  
Replication Protein A ◽  
Replication Protein ◽  
Iron Efficiency ◽  
A Subunit

Dynamics of Human Replication Protein A Subunit Distribution and Partitioning in the Cell Cycle

1996 ◽  
Vol 223 (2) ◽  
pp. 279-289 ◽  
Author(s):  
Kuruganti G. Murti ◽  
Da Cheng He ◽  
Bill R. Brinkley ◽  
Rebecca Scott ◽  
Suk-Hee Lee
Keyword(s):  
Cell Cycle ◽  
Protein A ◽  
Replication Protein A ◽  
Replication Protein ◽  
A Subunit

scholarly journals Determinants of replication protein A subunit interactions revealed using a phosphomimetic peptide

2020 ◽  
Vol 295 (52) ◽  
pp. 18449-18458
Author(s):  
Sungjin Lee ◽  
Jeongbeen Heo ◽  
Chin-Ju Park
Keyword(s):  
Protein A ◽  
Replication Protein A ◽  
Replication Protein ◽  
Domain Interaction ◽  
Docking Simulations ◽  
Ssdna Binding ◽  
Structural Details ◽  
Ssdna Binding Protein ◽  
A Subunit ◽  
Dna Resection

Replication protein A (RPA) is a eukaryotic ssDNA-binding protein and contains three subunits: RPA70, RPA32, and RPA14. Phosphorylation of the N-terminal region of the RPA32 subunit plays an essential role in DNA metabolism in processes such as replication and damage response. Phosphorylated RPA32 (pRPA32) binds to RPA70 and possibly regulates the transient RPA70-Bloom syndrome helicase (BLM) interaction to inhibit DNA resection. However, the structural details and determinants of the phosphorylated RPA32–RPA70 interaction are still unknown. In this study, we provide molecular details of the interaction between RPA70 and a mimic of phosphorylated RPA32 (pmRPA32) using fluorescence polarization and NMR analysis. We show that the N-terminal domain of RPA70 (RPA70N) specifically participates in pmRPA32 binding, whereas the unphosphorylated RPA32 does not bind to RPA70N. Our NMR data revealed that RPA70N binds pmRPA32 using a basic cleft region. We also show that at least 6 negatively charged residues of pmRPA32 are required for RPA70N binding. By introducing alanine mutations into hydrophobic positions of pmRPA32, we found potential points of contact between RPA70N and the N-terminal half of pmRPA32. We used this information to guide docking simulations that suggest the orientation of pmRPA32 in complex with RPA70N. Our study demonstrates detailed features of the domain-domain interaction between RPA70 and RPA32 upon phosphorylation. This result provides insight into how phosphorylation tunes transient bindings between RPA and its partners in DNA resection.

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