Transcription factor Runx1 recruits the polyomavirus replication origin to replication factories | JoVE Visualize

Transcription factor Runx1 recruits the polyomavirus replication origin to replication factories

Yota Murakami¹, Ling-Feng Chen, Noriyuki Sanechika

¹Department of Viral Oncology, Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan. yota@virus.kyoto-u.ac.jp

Journal of Cellular Biochemistry|October 26, 2006

View abstract on PubMed

Summary

Transcription factor Runx1 activates polyomavirus DNA replication by recruiting viral origins to replication factories. This process requires Runx1's nuclear matrix-binding activity for efficient viral DNA replication.

Area of Science:

Molecular Biology
Virology
Cell Biology

Background:

Eukaryotic DNA replication occurs in replication factories, requiring precise assembly of replication proteins.
The transcription factor Runx1 binds to the nuclear matrix, a key component of replication factories.
Previous studies demonstrated Runx1 activates polyomavirus DNA replication via its nuclear matrix-binding domain.

Purpose of the Study:

To elucidate the mechanism by which Runx1 activates polyomavirus DNA replication.
To investigate the role of Runx1 in recruiting viral replication origins to replication factories.

Main Methods:

Assessing the interaction of Runx1 with the nuclear matrix.
Evaluating the effect of Runx1 on the binding of polyomavirus large T antigen to its origin.
Analyzing the sub-cellular localization of newly replicated viral DNA, large T antigen, and Runx1 during replication.

Main Results:

Runx1 enhances the binding of polyomavirus large T antigen to the viral replication origin.
Newly replicated polyomavirus DNA and large T antigen are localized to replication factories on the nuclear matrix.
Runx1 co-localizes with large T antigen in replication factories during active, Runx1-dependent viral DNA replication.

Conclusions:

Runx1 facilitates polyomavirus DNA replication by recruiting viral origins to replication factories on the nuclear matrix.
The nuclear matrix-binding activity of Runx1 is essential for this recruitment and subsequent viral DNA replication.