JKMRS Volume 20, No 3, pp 66; NMR Study of Temperature-Depende... | |
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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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