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JKMRS Volume 20, No 3, pp 66; NMR Study of Temperature-Depende...
2016년 09월 20일 / 조회수: 649

NMR Study of Temperature-Dependent Single-Stranded DNA Binding

Affinity of Human Replication Protein A

 

 

Min-Gyu Kim1,, Tae-Hoan Shin1,, Seo-Ree Choi2, Jae-Gyu Choi1 and Joon-Hwa Lee2,*

 

 

 

1Gyeongnam Science High School, Jinju, Gyeongnam 52620, Republic of Korea

2Department of Chemistry and RINS, Gyeongsang National University, Jinju, Gyeongnam 52828, Republic of Korea

 

Received Aug10, 2016; Revised Sep 1, 2016; Accepted Sep2, 2016


Abstract The replication protein A (RPA), is a heterotrimer with 70, 32 and 14 kDa subunits and plays a crucial role in DNA replication, recombination, and repair. The largest subunit, RPA70, binds to single-stranded DNA (ssDNA) and mediates interactions with many cellular and viral proteins. In this study, we performed nuclear magnetic resonance experiments on the complex of the DNA binding domain A of human RPA70 (RPA70A) with ssDNA, d(CCCCC), at various temperatures, to understand the temperature dependency of ssDNA binding affinity of RPA70A. Essential residues for ssDNA binding were conserved while less essential parts were changed with the temperature. Our results provide valuable insights into the molecular mechanism of the ssDNA binding of human RPA.

 

Keywords RPA70A, ssDNA, DNA binding protein, temperature dependence, NMR

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