TRF2 recruits ORC through TRFH domain dimerization

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• 作者：Mitsunori Higa^a ; Tatsunori Kushiyama^a ; Seiichiro Kurashige^a ; Daisuke Kohmon^a ; Kouki Enokitani^a ; Satoko Iwahori^b ; Nozomi Sugimoto^a ; Kazumasa Yoshida^a ; ^{kyoshida@phar.kyushu-u.ac.jp} ; Masatoshi Fujita^a ; ^{mfujita@phar.kyushu-u.ac.jp}
• 关键词：TRF2 ; telomeric repeat binding factor 2 ; ORC ; origin recognition complex ; TRFH ; TRF homology ; pre-RC ; pre-replication complex ; G4 ; G-quadruplex ; TRF1 ; telomeric repeat binding factor 1 ; lacO ; lac operator ; LacI ; lac repressor ; ChIP ; chromatin immunoprecipitation ; qPCR ; quantitative real-time PCR ; H3K9me3 ; histone H3 trimethylated at K9 ; TERRA ; telomeric repeat-containing RNA
• 刊名：Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1864
• 期：1
• 页码：191-201
• 全文大小：1679 K
• 卷排序：1864

文摘

TRF2 is thought to mediate ORC recruitment to the telomeric replication origins. Tethering of TRF2 by LacI fusion to a lacO array induces ORC recruitment. The TRFH domain of TRF2 is sufficient to recruit ORC and pre-RC onto the lacO array. The recruitment of ORC and pre-RC is dependent on dimerization of the TRFH domain. Dimerized TRFH domain binds to ORC via a direct interaction with the ORC1 subunit.