JANOUŠKOVÁ, Eliška, Ivona NEČASOVÁ, Jana PAVLOUŠKOVÁ, Michal ZIMMERMANN, Milan HLUCHÝ, María Victoria MARINI PALOMEQUE, Monika NOVÁKOVÁ and Ctirad HOFR. Human Rap1 modulates TRF2 attraction to telomeric DNA. Nucleic Acids Research. Oxford: Oxford University Press, 2015, vol. 43, No 5, p. 2691-2700. ISSN 0305-1048. doi:10.1093/nar/gkv097.
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Basic information
Original name Human Rap1 modulates TRF2 attraction to telomeric DNA
Authors JANOUŠKOVÁ, Eliška (203 Czech Republic, belonging to the institution), Ivona NEČASOVÁ (203 Czech Republic, belonging to the institution), Jana PAVLOUŠKOVÁ (203 Czech Republic, belonging to the institution), Michal ZIMMERMANN (203 Czech Republic, belonging to the institution), Milan HLUCHÝ (703 Slovakia, belonging to the institution), María Victoria MARINI PALOMEQUE (858 Uruguay, belonging to the institution), Monika NOVÁKOVÁ (203 Czech Republic, belonging to the institution) and Ctirad HOFR (203 Czech Republic, guarantor, belonging to the institution).
Edition Nucleic Acids Research, Oxford, Oxford University Press, 2015, 0305-1048.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 9.202
RIV identification code RIV/00216224:14740/15:00081706
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1093/nar/gkv097
UT WoS 000352487100024
Tags podil, rivok
Changed by Changed by: Mgr. Eva Špillingová, učo 110713. Changed: 21. 4. 2016 13:15.
More than two decades of genetic research have identified and assigned main biological functions of shelterin proteins that safeguard telomeres. However, a molecular mechanism of how each protein subunit contributes to the protecting function of the whole shelterin complex remains elusive. Human Repressor activator protein 1 (Rap1) forms a multifunctional complex with Telomeric Repeat binding Factor 2 (TRF2). Rap1-TRF2 complex is a critical part of shelterin as it suppresses homology-directed repair in Ku 70/80 heterodimer absence. To understand how Rap1 affects key functions of TRF2, we investigated full-length Rap1 binding to TRF2 and Rap1-TRF2 complex interactions with double-stranded DNA by quantitative biochemical approaches. We observed that Rap1 reduces the overall DNA duplex binding affinity of TRF2 but increases the selectivity of TRF2 to telomeric DNA. Additionally, we observed that Rap1 induces a partial release of TRF2 from DNA duplex. The improved TRF2 selectivity to telomeric DNA is caused by less pronounced electrostatic attractions between TRF2 and DNA in Rap1 presence. Thus, Rap1 prompts more accurate and selective TRF2 recognition of telomeric DNA and TRF2 localization on single/double-strand DNA junctions. These quantitative functional studies contribute to the understanding of the selective recognition of telomeric DNA by the whole shelterin complex.
ED1.1.00/02.0068, research and development projectName: CEITEC - central european institute of technology
GAP205/12/0550, research and development projectName: Dynamika vzniku shelterinového komplexu
Investor: Czech Science Foundation
GAP207/12/2323, research and development projectName: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I
Investor: Czech Science Foundation
GA13-26693S, research and development projectName: Genetická diverzita a fylogeneze rodu Acinetobacter v přírodních ekosystémech.
Investor: Czech Science Foundation
LH13054, research and development projectName: Studium dynamiky telomerových proteinových komplexů zajišťujících stabilitu genomu (Acronym: TeloProtGen)
Investor: Ministry of Education, Youth and Sports of the CR
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