Detailed Information on Publication Record
2019
Human Telomere Repeat Binding Factor TRF1 Replaces TRF2 Bound to Shelterin Core Hub TIN2 when TPP1 Is Absent
JANOVIČ, Tomáš, Martin STOJASPAL, Pavel VEVERKA, Denisa HORÁKOVÁ, Ctirad HOFR et. al.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
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10610 Biophysics
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 4.760
RIV identification code
RIV/00216224:14310/19:00107497
Organization unit
Faculty of Science
UT WoS
000482872100020
Keywords in English
TIN2; telomere; shelterin; assembly; single-molecule
Tags
International impact, Reviewed
Změněno: 3/3/2020 16:31, Mgr. Pavla Foltynová, Ph.D.
Abstract
V originále
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 project |
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| GA19-18226S, research and development project |
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| LM2015043, research and development project |
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| LM2015051, research and development project |
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| LQ1601, research and development project |
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