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ORC binding to TRF2 stimulates OriP replication
Author(s) -
Atanasiu Constandache,
Deng Zhong,
Wiedmer Andreas,
Norseen Julie,
Lieberman Paul M
Publication year - 2006
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400730
Subject(s) - origin recognition complex , biology , origin of replication , dna replication , pre replication complex , minichromosome maintenance , seqa protein domain , replication factor c , control of chromosome duplication , dna , dna replication factor cdt1 , eukaryotic dna replication , telomere , microbiology and biotechnology , plasmid , genetics
In higher eukaryotes, the origin recognition complex (ORC) lacks sequence‐specific DNA binding, and it remains unclear what other factors specify an origin of DNA replication. The Epstein–Barr virus origin of plasmid replication (OriP) recruits ORC, but the precise mechanism of ORC recruitment and origin activation is not clear. We now show that ORC is recruited selectively to the dyad symmetry (DS) region of OriP as a consequence of direct interactions with telomere repeat factor 2 (TRF2) and ORC1. TRF‐binding sites within DS stimulate replication initiation and facilitate ORC recruitment in vitro and in vivo . TRF2, but not TRF1 or hRap1, recruits ORC from nuclear extracts. The amino‐terminal domain of TRF2 associated with a specific region of ORC1 and was necessary for stimulation of DNA replication. These results support a model in which TRF2 stimulates OriP replication activity by direct binding with ORC subunits.