TRF2 recruits ORC through TRFH domain dimerization.
作者： Mitsunori Higa , Tatsunori Kushiyama , Seiichiro Kurashige , Daisuke Kohmon , Kouki Enokitani
DOI: 10.1016/J.BBAMCR.2016.11.004
关键词: Minichromosome maintenance 、 Molecular biology 、 Pre-replication complex 、 Chromatin binding 、 Cell biology 、 Biology 、 DNA replication 、 Origin recognition complex 、 Telomerase 、 Chromatin 、 Eukaryotic DNA replication
摘要: Telomeres are specialized chromatin structures that prevent the degradation and instability of ends linear chromosomes. While telomerase maintains long stretches telomeric repeat, majority DNA is duplicated by conventional replication. A fundamental step in eukaryotic replication involves binding origin recognition complex (ORC). In human cells, repeat factor 2 (TRF2) thought to play a role recruitment ORC onto telomeres. To better understand mechanism TRF2-mediated recruitment, we utilized lacO-LacI protein tethering system U2OS cells found ectopically targeted TRF2, but not TRF1, can recruit lacO array. We further TRF homology (TRFH) dimerization domain its mutant defective dimerization, sufficient for minichromosome maintenance (MCM) recruitment. Mutations impairing also compromised full-length TRF2. Similar results were obtained using immunoprecipitation GST pull-down assays. Together, these suggest dimerized TRF2 recruits stimulates pre-replication (pre-RC) formation at telomeres through TRFH domain.
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