NMR studies on the interaction of Replication Protein A 32 (RPA32) and TIPIN = RPA32 와 TIPIN 의 상호작용에 대한 NMR 연구

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The RPA32 protein is involved in various DNA repair systems such as nucleotide excision repair (NER), base excision repair (BER), and homologous recombination. In these processes, RPA32 interacts with different binding partners at its C terminal common binding site (172-270; RPA32C). It has been reported recently that RPA32C also interacts with TIPIN during the intra-S checkpoint. During S phase TIM-TIPIN complex is present in replication foci and RPA32 facilitate the complex near the replication fork during the intra-S checkpoint. RPA32 facilitates the TIM-TIPIN complex, by direct interacting with TIPIN and the checkpoint response alleviates efficiently during the checkpoint response. Here, we show that TIPIN(185-218), which shares high sequence similarity with XPA(10-43) and UNG2(56-89), is disordered in free state and becomes structured upon binding to RPA32C with accompanying helix formation. The binding interface between TIPIN(185-218) and RPA32C is not exactly similar rather it has two binding sites compared to those of XPA- and UNG2-RPA32C complexes. Also, the binding affinities of those proteins towards RPA32C are comparable suggesting that DNA repair, homologous recombination, and checkpoint processes regulated by RPA32 in a competitive manner with comparable binding affinity.
Advisors
Choi, Byong-Seokresearcher최병석researcher
Description
한국과학기술원 : 화학과,
Publisher
한국과학기술원
Issue Date
2010
Identifier
418843/325007  / 020044501
Language
eng
Description

학위논문(박사) - 한국과학기술원 : 화학과, 2010.2, [ vii, 73 p. ]

Keywords

DNA Repair; TIPIN; RPA32; NMR spectroscopy; Protein-protein Interaction; 단백질-단백질 상호작용; DNA 회복; TIPIN; RPA32; NMR

URI
http://hdl.handle.net/10203/31754
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=418843&flag=dissertation
Appears in Collection
CH-Theses_Ph.D.(박사논문)
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