Subcellular localization of RPB5-mediating protein and its putative functional partner

Molecular and Cellular Biology
Luvsanjav DelgermaaSeishi Murakami

Abstract

We previously identified a novel cellular protein, RPB5-mediating protein (RMP), that retains corepressor activity and functionally antagonizes transcriptional modulation via hepatitis B virus X protein. The subcellular localization of RMP was examined using green fluorescent protein-fused protein forms. We found that a nuclear localization signal (NLS) and a coiled-coil (CC) domain functioning as a cytoplasmic localization signal (CLS) are important for the subcellular localization of RMP. The CLS apparently acts dominantly, since RMP was mostly localized in the cytoplasm with weak and diffuse signals in the nucleus, and the NLS was indispensable for the nuclear localization of RMP only in the absence of the CLS. Using a yeast two-hybrid method, we isolated a putative corepressor, DNA methyltransferase 1-associating protein (DMAP1), which was found to bind to the CC domain of RMP. DMAP1 facilitated the nuclear localization of RMP and the corepressor activity of RMP in a dose-dependent manner by interacting with the CC domain of RMP. These results are discussed in light of a recent paper showing a novel evolutionarily conserved role of URI in the TOR signaling pathway.

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Jul 7, 2011·Molecular and Cellular Biology·Paolo MitaSusan K Logan
May 11, 2010·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Philippe Cloutier, Benoit Coulombe
Mar 6, 2013·PLoS Genetics·María Carmen Mirón-GarcíaFrancisco Navarro
Jul 13, 2013·International Journal of Biological Sciences·Sijun YangWenxiang Wei
Jul 11, 2014·Open Biology·Gonzalo Millán-Zambrano, Sebastián Chávez
Aug 2, 2014·Nucleic Acids Research·María Carmen Mirón-GarcíaFrancisco Navarro
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