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Transcription factor Runx1 recruits the polyomavirus replication origin to replication factories
Author(s) -
Murakami Yota,
Chen LingFeng,
Sanechika Noriyuki,
Kohzaki Hidetsugu,
Ito Yoshiaki
Publication year - 2006
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.21115
Subject(s) - control of chromosome duplication , origin recognition complex , replication factor c , dna replication factor cdt1 , eukaryotic dna replication , licensing factor , dna replication , minichromosome maintenance , biology , pre replication complex , origin of replication , s phase , microbiology and biotechnology , genetics , dna
Eukaryotic DNA replication takes place in the replication factories, where replication proteins are properly assembled to form replication forks. Thus, recruitment of DNA replication origins to the replication factories must be the key step for the regulation of DNA replication. The transcription factor Runx1 associates with the nuclear matrix, the putative substructure of DNA replication factories. An earlier report from our laboratory showed that Runx1 activates polyomavirus DNA replication, and that this requires its nuclear matrix‐binding activity. Here, we show that Runx1 activates polyomavirus DNA replication by stimulating the binding of the viral‐encoded replication initiator/helicase, large T antigen, to its replication origin. We found that newly replicated polyomavirus DNA is associated with the nuclear matrix and that large T antigen is targeted to replication factories, suggesting that polyomavirus is replicated in replication factories on the nuclear matrix. Although Runx1 did not co‐localize with large T antigen‐containing foci by itself, it co‐localized with large T antigen‐containing replication factories during Runx1‐dependent polyomavirus DNA replication. These observations together suggest that Runx1 recruits the polyomavirus replication origin to the replication factory on the nuclear matrix, and that this requires the nuclear matrix‐binding activity of Runx1. J. Cell. Biochem. 100: 1313–1323, 2007. © 2006 Wiley‐Liss, Inc.