Rtf1-mediated eukaryotic site-specific replication termination.

Genetics
T EydmannJacob Z Dalgaard

Abstract

The molecular mechanisms mediating eukaryotic replication termination and pausing remain largely unknown. Here we present the molecular characterization of Rtf1 that mediates site-specific replication termination at the polar Schizosaccharomyces pombe barrier RTS1. We show that Rtf1 possesses two chimeric myb/SANT domains: one is able to interact with the repeated motifs encoded by the RTS1 element as well as the elements enhancer region, while the other shows only a weak DNA binding activity. In addition we show that the C-terminal tail of Rtf1 mediates self-interaction, and deletion of this tail has a dominant phenotype. Finally, we identify a point mutation in Rtf1 domain I that converts the RTS1 element into a replication barrier of the opposite polarity. Together our data establish that multiple protein DNA and protein-protein interactions between Rtf1 molecules and both the repeated motifs and the enhancer region of RTS1 are required for site-specific termination at the RTS1 element.

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Citations

May 7, 2009·Proceedings of the National Academy of Sciences of the United States of America·Takabumi InagawaJacob Z Dalgaard
Oct 25, 2012·PLoS Genetics·Ismail IraquiSarah A E Lambert
Nov 4, 2009·FEBS Letters·Stefan Vörtler, Mario Mörl
Oct 6, 2015·Nature Structural & Molecular Biology·Izumi MiyabeAntony M Carr
Mar 21, 2009·Molecular Microbiology·Daniel L Kaplan, Deepak Bastia
Apr 2, 2016·Proceedings of the National Academy of Sciences of the United States of America·Rahul JaiswalCarlos R Escalante
Apr 14, 2016·Current Genetics·Mariana C GadaletaEishi Noguchi
Dec 25, 2012·Cell Reports·Allyson HolmesBenoit Arcangioli
May 6, 2014·Seminars in Cell & Developmental Biology·Jagmohan Singh
Jun 15, 2016·Proceedings of the National Academy of Sciences of the United States of America·Deepak BastiaMichael E O'Donnell
Dec 2, 2010·Journal of Cell Science·Leonor Rodríguez-SánchezPablo Hernández

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