JANOVIČ, Tomáš, Martin STOJASPAL, Pavel VEVERKA, Denisa HORÁKOVÁ and Ctirad HOFR. Human Telomere Repeat Binding Factor TRF1 Replaces TRF2 Bound to Shelterin Core Hub TIN2 when TPP1 Is Absent. Journal of Molecular Biology. London: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, 2019, vol. 431, No 17, p. 3289-3301. ISSN 0022-2836. Available from: https://dx.doi.org/10.1016/j.jmb.2019.05.038.
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Basic information
Original name Human Telomere Repeat Binding Factor TRF1 Replaces TRF2 Bound to Shelterin Core Hub TIN2 when TPP1 Is Absent
Authors JANOVIČ, Tomáš (203 Czech Republic, belonging to the institution), Martin STOJASPAL (203 Czech Republic, belonging to the institution), Pavel VEVERKA (203 Czech Republic, belonging to the institution), Denisa HORÁKOVÁ (203 Czech Republic, belonging to the institution) and Ctirad HOFR (203 Czech Republic, guarantor, belonging to the institution).
Edition Journal of Molecular Biology, London, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, 2019, 0022-2836.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10610 Biophysics
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW Full Text
Impact factor Impact factor: 4.760
RIV identification code RIV/00216224:14310/19:00107497
Organization unit Faculty of Science
Doi http://dx.doi.org/10.1016/j.jmb.2019.05.038
UT WoS 000482872100020
Keywords in English TIN2; telomere; shelterin; assembly; single-molecule
Tags CF BIC, CF PROT, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 3/3/2020 16:31.
Abstract
Human telomeric repeat binding factors TRF1 and TRF2 along with TIN2 form the core of the shelterin complex that protects chromosome ends against unwanted end-joining and DNA repair. We applied a single-molecule approach to assess TRF1–TIN2–TRF2 complex formation in solution at physiological conditions. Fluorescence cross-correlation spectroscopy was used to describe the complex assembly by analyzing how coincident fluctuations of differently labeled TRF1 and TRF2 correlate when they move together through the confocal volume of the microscope. We observed, at the single-molecule level, that TRF1 effectively substitutes TRF2 on TIN2. We assessed also the effect of another telomeric factor TPP1 that recruits telomerase to telomeres. We found that TPP1 upon binding to TIN2 induces changes that expand TIN2 binding capacity, such that TIN2 can accommodate both TRF1 and TRF2 simultaneously. We suggest a molecular model that explains why TPP1 is essential for the stable formation of TRF1–TIN2–TRF2 core complex.
Links
GA16-20255S, research and development projectName: Molekulární mechanismus inhibice telomerázy: cílené zastavení dělení nádorových buněk
Investor: Czech Science Foundation
GA19-18226S, research and development projectName: Kritické interakce neuronového transkripčního faktoru REST se stabilizátorem TRF2: biofyzikální implikace pro návrh léčiv glioblastomu
Investor: Czech Science Foundation
LM2015043, research and development projectName: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)
Investor: Ministry of Education, Youth and Sports of the CR
LM2015051, research and development projectName: Centrum pro výzkum toxických látek v prostředí (Acronym: RECETOX RI)
Investor: Ministry of Education, Youth and Sports of the CR
LQ1601, research and development projectName: CEITEC 2020 (Acronym: CEITEC2020)
Investor: Ministry of Education, Youth and Sports of the CR
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