TRF1 and TRF2 use different mechanisms to find telomeric DNA but share a novel mechanism to search for protein partners at telomeres
DC Element | Wert | Sprache |
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dc.contributor.author | Lin, Jiangguo | |
dc.contributor.author | Countryman, Preston | |
dc.contributor.author | Buncher, Noah | |
dc.contributor.author | Kaur, Parminder | |
dc.contributor.author | Longjiang, E. | |
dc.contributor.author | Zhang, Yiyun | |
dc.contributor.author | Gibson, Greg | |
dc.contributor.author | You, Changjiang | |
dc.contributor.author | Watkins, Simon C. | |
dc.contributor.author | Piehler, Jacob | |
dc.contributor.author | Opresko, Patricia L. | |
dc.contributor.author | Kad, Neil M. | |
dc.contributor.author | Wang, Hong | |
dc.date.accessioned | 2021-12-23T16:22:47Z | - |
dc.date.available | 2021-12-23T16:22:47Z | - |
dc.date.issued | 2014 | |
dc.identifier.issn | 03051048 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/14305 | - |
dc.description.abstract | Human telomeres are maintained by the shelterin protein complex in which TRF1 and TRF2 bind directly to duplex telomeric DNA. How these proteins find telomeric sequences among a genome of billions of base pairs and how they find protein partners to form the shelterin complex remains uncertain. Using single-molecule fluorescence imaging of quantum dot-labeled TRF1 and TRF2, we study how these proteins locate TTAGG G repeats on DNA tightropes. By virtue of its basic domain TRF2 performs an extensive 1D search on nontelomeric DNA, whereas TRF1's 1D search is limited. Unlike the stable and static associations observed for other proteins at specific binding sites, TRF proteins possess reduced binding stability marked by transient binding (similar to 9-17 s) and slow 1D diffusion on specific telomeric regions. These slow diffusion constants yield activation energy barriers to sliding similar to 2.8-3.6 kappa T-B greater than those for nontelomeric DNA. We propose that the TRF proteins use 1D sliding to find protein partners and assemble the shelterin complex, which in turn stabilizes the interaction with specific telomeric DNA. This `tag-team proofreading' represents a more general mechanism to ensure a specific set of proteins interact with each other on long repetitive specific DNA sequences without requiring external energy sources. | |
dc.description.sponsorship | BBSRCUK Research & Innovation (UKRI)Biotechnology and Biological Sciences Research Council (BBSRC) [BB/I003460/1]; National Institutes of HealthUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USA [ES0515052, 4R00ES016758]; Biotechnology and Biological Sciences Research CouncilUK Research & Innovation (UKRI)Biotechnology and Biological Sciences Research Council (BBSRC) [BB/I003460/1] Funding Source: researchfish; NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Environmental Health Sciences (NIEHS) [R00ES016758, R01ES015052] Funding Source: NIH RePORTER; NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [U54GM103529] Funding Source: NIH RePORTER; The BBSRC [BB/I003460/1 to N.M.K.]; National Institutes of Health [ES0515052 to P.L.O. and 4R00ES016758 to H.W.]. Funding for open access charges: National Institutes of Health [4R00ES016758]. | |
dc.language.iso | en | |
dc.publisher | OXFORD UNIV PRESS | |
dc.relation.ispartof | NUCLEIC ACIDS RESEARCH | |
dc.subject | BINDING | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | DRIVEN MECHANISMS | |
dc.subject | END | |
dc.subject | FACILITATED TARGET LOCATION | |
dc.subject | MOLECULE IMAGING REVEALS | |
dc.subject | NUCLEIC-ACIDS | |
dc.subject | ONE-DIMENSIONAL DIFFUSION | |
dc.subject | SINGLE-PARTICLE TRACKING | |
dc.subject | SITE | |
dc.subject | TRANSLOCATION | |
dc.title | TRF1 and TRF2 use different mechanisms to find telomeric DNA but share a novel mechanism to search for protein partners at telomeres | |
dc.type | journal article | |
dc.identifier.doi | 10.1093/nar/gkt1132 | |
dc.identifier.isi | ISI:000332381000041 | |
dc.description.volume | 42 | |
dc.description.issue | 4 | |
dc.description.startpage | 2493 | |
dc.description.endpage | 2504 | |
dc.contributor.orcid | 0000-0002-7839-6397 | |
dc.contributor.orcid | 0000-0003-4092-1552 | |
dc.contributor.orcid | 0000-0003-0165-3559 | |
dc.contributor.orcid | 0000-0001-9183-4315 | |
dc.contributor.orcid | 0000-0002-3491-8595 | |
dc.contributor.orcid | 0000-0002-6470-2189 | |
dc.contributor.researcherid | L-3901-2014 | |
dc.contributor.researcherid | ABG-2590-2021 | |
dc.contributor.researcherid | F-3164-2014 | |
dc.identifier.eissn | 13624962 | |
dc.publisher.place | GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND | |
dcterms.isPartOf.abbreviation | Nucleic Acids Res. | |
dcterms.oaStatus | gold, Green Published, Green Accepted, Green Submitted | |
crisitem.author.dept | Sonderforschungsbereich 944: Physiologie und Dynamik zellulärer Mikrokompartimente | - |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | organisation19 | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.orcid | 0000-0002-7839-6397 | - |
crisitem.author.orcid | 0000-0002-2143-2270 | - |
crisitem.author.parentorg | FB 05 - Biologie/Chemie | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.grandparentorg | Universität Osnabrück | - |
crisitem.author.netid | YoCh745 | - |
crisitem.author.netid | PiJa938 | - |
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geprüft am 10.05.2024