The N-terminal domain of the large subunit of human replication protein A binds to Werner syndrome protein and stimulates helicase activity

2003 ◽  
Vol 124 (8-9) ◽  
pp. 921-930 ◽  
Author(s):  
Jiang-Cheng Shen ◽  
Ye Lao ◽  
Ashwini Kamath-Loeb ◽  
Marc S. Wold ◽  
Lawrence A. Loeb
Keyword(s):  
Werner Syndrome ◽  
Large Subunit ◽  
Protein A ◽  
Replication Protein A ◽  
Replication Protein ◽  
Helicase Activity ◽  
Terminal Domain ◽  
Werner Syndrome Protein ◽  
Syndrome Protein

scholarly journals Replication Protein A Stimulates the Werner Syndrome Protein Branch Migration Activity

2009 ◽  
Vol 284 (50) ◽  
pp. 34682-34691 ◽  
Author(s):  
Gregory Sowd ◽  
Hong Wang ◽  
Dalyir Pretto ◽  
Walter J. Chazin ◽  
Patricia L. Opresko
Keyword(s):  
Werner Syndrome ◽  
Protein A ◽  
Replication Protein A ◽  
Replication Protein ◽  
Branch Migration ◽  
Migration Activity ◽  
Werner Syndrome Protein ◽  
Syndrome Protein

scholarly journals Inhibition of Werner Syndrome Helicase Activity by Benzo[a]pyrene Diol Epoxide Adducts Can Be Overcome by Replication Protein A

2005 ◽  
Vol 281 (9) ◽  
pp. 6000-6009 ◽  
Author(s):  
Saba Choudhary ◽  
Kevin M. Doherty ◽  
Christopher J. Handy ◽  
Jane M. Sayer ◽  
Haruhiko Yagi ◽  
...  
Keyword(s):  
Werner Syndrome ◽  
Protein A ◽  
Replication Protein A ◽  
Replication Protein ◽  
Helicase Activity ◽  
Diol Epoxide

scholarly journals Investigation of the core binding regions of human Werner syndrome and Fanconi anemia group J helicases on replication protein A

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Gyuho Yeom ◽  
Jinwoo Kim ◽  
Chin-Ju Park
Keyword(s):  
Fanconi Anemia ◽  
Protein Interactions ◽  
Werner Syndrome ◽  
Protein A ◽  
Replication Protein A ◽  
Replication Protein ◽  
Dna Helicases ◽  
Binding Regions ◽  
Werner Syndrome Protein ◽  
Anemia Group

Abstract Werner syndrome protein (WRN) and Fanconi anemia group J protein (FANCJ) are human DNA helicases that contribute to genome maintenance. They interact with replication protein A (RPA), and these interactions dramatically enhance the unwinding activities of both helicases. Even though the interplay between these helicases and RPA is particularly important in the chemoresistance pathway of cancer cells, the precise binding regions, interfaces, and properties have not yet been characterized. Here we present systematic NMR analyses and fluorescence polarization anisotropy assays of both helicase-RPA interactions for defining core binding regions and binding affinities. Our results showed that two acidic repeats of human WRN bind to RPA70N and RPA70A. For FANCJ, the acidic-rich sequence in the C-terminal domain is the binding region for RPA70N. Our results suggest that each helicase interaction has unique features, although they both fit an acidic peptide into a basic cleft for RPA binding. Our findings shed light on the protein interactions involved in overcoming the DNA-damaging agents employed in the treatment of cancer and thus potentially provide insight into enhancing the efficacy of cancer therapy.

scholarly journals Replication Protein A Physically Interacts with the Bloom's Syndrome Protein and Stimulates Its Helicase Activity

2000 ◽  
Vol 275 (31) ◽  
pp. 23500-23508 ◽  
Author(s):  
Robert M. Brosh ◽  
Ji-Liang Li ◽  
Mark K. Kenny ◽  
Julia K. Karow ◽  
Marcus P. Cooper ◽  
...  
Keyword(s):  
Protein A ◽  
Replication Protein A ◽  
Replication Protein ◽  
Helicase Activity ◽  
Bloom's Syndrome ◽  
Bloom’S Syndrome ◽  
Syndrome Protein

scholarly journals Interaction of replication protein A with two acidic peptides from human Bloom syndrome protein

FEBS Letters ◽  
2018 ◽  
Vol 592 (4) ◽  
pp. 547-558 ◽  
Author(s):  
Donguk Kang ◽  
Sungjin Lee ◽  
Kyoung‐Seok Ryu ◽  
Hae‐Kap Cheong ◽  
Eun‐Hee Kim ◽  
...  
Keyword(s):  
Protein A ◽  
Replication Protein A ◽  
Bloom Syndrome ◽  
Replication Protein ◽  
Syndrome Protein ◽  
Acidic Peptides
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