| NEČASOVÁ, Ivona, Eliška JANOUŠKOVÁ, Tomáš KLUMPLER and Ctirad HOFR. Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it. Nucleic Acids Research. 2017, vol. 45, No 21, p. 12170-12180. ISSN 0305-1048. Available from: 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 and Ctirad HOFR. Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it. \textit{Nucleic Acids Research}. 2017, vol.~45, No~21, p.~12170-12180. ISSN~0305-1048. Available from: https://dx.doi.org/10.1093/nar/gkx812.
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