Recognition of cisplatin-DNA interstrand cross-links by replication protein A

Biochemistry
Steve M PatrickJeffrey M Horn

Abstract

Replication protein A (RPA) is a heterotrimeric protein that is required for DNA replication and most DNA repair pathways. RPA has previously been shown to play a role in recognizing and binding damaged DNA during nucleotide excision repair (NER). RPA has also been suggested to play a role in psoralen DNA interstrand cross-link (ICL) repair, but a clear biochemical activity has yet to be identified in the ICL DNA repair pathways. Using HeLa cell extracts and DNA affinity chromatography, we demonstrate that RPA is preferentially retained on a cisplatin interstrand cross-link (ICL) DNA column compared with undamaged DNA. The retention of RPA on cisplatin intrastrand and ICL containing DNA affinity columns is comparable. In vitro electrophoretic mobility shift assays (EMSAs) using synthetic DNA substrates and purified RPA demonstrate higher affinity for cisplatin ICL DNA binding compared with undamaged DNA. The enhanced binding of RPA to the cisplatin ICL is dependent on the DNA length. As the DNA flanking the cisplatin ICL is increased from 7 to 21 bases, preferential RPA binding is observed. Fluorescence anisotropy reveals greater than 200-fold higher affinity to a cisplatin ICL containing 42-mer DNA compared with an undamaged D...Continue Reading

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Citations

Mar 2, 2011·The Journal of Biological Chemistry·Anbarasi KothandapaniSteve M Patrick
Jun 14, 2013·Nucleic Acids Research·Anbarasi KothandapaniSteve M Patrick
Dec 29, 2010·Journal of Nucleic Acids·Victor J Anciano GranadilloJohn J Turchi
Nov 12, 2015·International Journal of Molecular Sciences·Gaëlle Savreux-LengletMarie-Hélène David-Cordonnier
Dec 3, 2014·Cancer Treatment Reviews·Shane O'GradyMartin P Barr
Dec 31, 2009·Critical Reviews in Biochemistry and Molecular Biology·Parameswary A MuniandyMichael M Seidman
Oct 26, 2016·International Journal of Oncology·Shu-Yuan ChengElise Champeil

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