Retrotransposon Tf1 is targeted to Pol II promoters by transcription activators.

Molecular Cell
Young-Eun LeemHenry L Levin

Abstract

The LTR-retrotransposon Tf1 preserves the coding capacity of its host Schizosaccharomyces pombe by integrating upstream of open reading frames (ORFs). To determine which features of the target sites were recognized by the transposon, we introduced plasmids containing candidate insertion sites into S. pombe and mapped the positions of integration. We found that Tf1 was targeted specifically to the promoters of Pol II-transcribed genes. A detailed analysis of integration in plasmids that contained either ade6 or fbp1 revealed insertions occurred in the promoters at positions where transcription factors bound. Further experiments revealed that the activator Atf1p and its binding site were required for directing integration to the promoter of fbp1. An interaction between Tf1 integrase and Atf1p was observed, indicating that integration at fbp1 was mediated by the activator bound to its promoter. Surprisingly, we found Tf1 contained sequences that activated transcription, and these substituted for elements of the ade6 promoter disrupted by integration.

References

Jan 17, 2003·Molecular Biology of the Cell·Dongrong ChenJürg Bähler
May 6, 2003·Proceedings of the National Academy of Sciences of the United States of America·Yunxia ZhuDaniel F Voytas
Nov 29, 2005·Nature Medicine·Angela CiuffiFrederic Bushman
Mar 14, 2007·Annual Review of Biochemistry·Yao-Fu ChangMiles F Wilkinson
Aug 3, 2007·Genes & Development·Olaf Isken, Lynne E Maquat
Aug 19, 2007·PLoS Genetics·Alfica SehgalPeter J Espenshade

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Citations

Aug 19, 2011·Nature Reviews. Genetics·Henry L Levin, John V Moran
Feb 6, 2010·Proceedings of the National Academy of Sciences of the United States of America·Andrea L FerrisStephen H Hughes
Jul 27, 2011·Proceedings of the National Academy of Sciences of the United States of America·Joshua A BallerDaniel F Voytas
Apr 12, 2012·The Journal of Biological Chemistry·Xiaojie Qi, Suzanne Sandmeyer
Aug 12, 2009·The Journal of Heredity·Ellen J Pritham
Oct 28, 2008·Nucleic Acids Research·Anja O PaateroHarri Savilahti
Nov 28, 2008·Nucleic Acids Research·Eugene ValkovPeter Cherepanov
Nov 30, 2012·Nucleic Acids Research·Gang FengHenry L Levin
Dec 26, 2008·Journal of Virology·Atreyi Ghatak ChatterjeeHenry L Levin
Aug 6, 2008·Annual Review of Genetics·Arthur BeauregardMarlene Belfort
Jul 23, 2013·PloS One·Kenji K Kojima, Jerzy Jurka
Jul 3, 2013·Proceedings of the National Academy of Sciences of the United States of America·Amit SharmaMamuka Kvaratskhelia
Oct 29, 2015·Critical Reviews in Biochemistry and Molecular Biology·Erik Serrao, Alan N Engelman
Jun 3, 2014·The Journal of Physiology·James A Shapiro
Aug 9, 2011·Comptes rendus biologies·Claudine Bleykasten-Grosshans, Cécile Neuvéglise
Sep 26, 2015·Science·Jake Z JacobsMikel Zaratiegui
Jun 10, 2014·Frontiers in Genetics·Tobias MourierEske Willerslev
Jun 21, 2014·Nucleic Acids Research·Atreyi Ghatak ChatterjeeHenry L Levin
Nov 22, 2016·Nature Reviews. Genetics·Edward B ChuongCédric Feschotte
Mar 14, 2017·Nature Reviews. Genetics·Tania SultanaPascale Lesage
Dec 14, 2018·Genome Research·Caroline EsnaultHenry L Levin
Nov 22, 2013·Biochemical Society Transactions·Mikel Zaratiegui
Aug 28, 2016·Genome Biology and Evolution·Amir SzitenbergDavid H Lunt
Sep 22, 2020·Annual Review of Genetics·Jonathan N Wells, Cédric Feschotte
Sep 10, 2015·Microbiology Spectrum·Caroline Esnault, Henry L Levin

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