NEČASOVÁ, Ivona, Eliška JANOUŠKOVÁ, Tomáš KLUMPLER a Ctirad HOFR. Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it. Nucleic Acids Research. 2017, roč. 45, č. 21, s. 12170-12180. ISSN 0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gkx812. |
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@article{1394029, author = {Nečasová, Ivona and Janoušková, Eliška and Klumpler, Tomáš and Hofr, Ctirad}, article_number = {21}, doi = {http://dx.doi.org/10.1093/nar/gkx812}, keywords = {TRF2; DNA; telomere; D-loop; Rap1}, language = {eng}, issn = {0305-1048}, journal = {Nucleic Acids Research}, title = {Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it}, url = {http://www.lablifeb.org}, volume = {45}, year = {2017} }
TY - JOUR ID - 1394029 AU - Nečasová, Ivona - Janoušková, Eliška - Klumpler, Tomáš - Hofr, Ctirad PY - 2017 TI - Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it JF - Nucleic Acids Research VL - 45 IS - 21 SP - 12170-12180 EP - 12170-12180 SN - 03051048 KW - TRF2 KW - DNA KW - telomere KW - D-loop KW - Rap1 UR - http://www.lablifeb.org L2 - https://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkx812 N2 - Telomeric repeat binding factor 2 (TRF2) folds human telomeres into loops to prevent unwanted DNA repair and chromosome end-joining. The N-terminal basic domain of TRF2 (B-domain) protects the telomeric displacement loop (D-loop) from cleavage by endonucleases. Repressor activator protein 1 (Rap1) binds TRF2 and improves telomeric DNA recognition. We found that the B-domain of TRF2 stabilized the D-loop and thus reduced unwinding by BLM and RPA, whereas the formation of the Rap1–TRF2 complex restored DNA unwinding. To understand how the B-domain of TRF2 affects DNA binding and D-loop processing, we analyzed DNA binding of full-length TRF2 and a truncated TRF2 construct lacking the B-domain. We quantified how the B-domain improves TRF2’s interaction with DNA via enhanced long-range electrostatic interactions. We developed a structural envelope model of the B-domain bound on DNA. The model revealed that the B-domain is flexible in solution but becomes rigid upon binding to telomeric DNA. We proposed a mechanism for how the B-domain stabilizes the D-loop. ER -
NEČASOVÁ, Ivona, Eliška JANOUŠKOVÁ, Tomáš KLUMPLER a Ctirad HOFR. Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it. \textit{Nucleic Acids Research}. 2017, roč.~45, č.~21, s.~12170-12180. ISSN~0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gkx812.
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