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Reptin and Pontin function antagonistically with PcG and TrxG complexes to mediate Hox gene control

Academic Article
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Overview

authors

  • Diop, S. B.
  • Bertaux, K.
  • Vasanthi, D.
  • Sarkeshik, A.
  • Goirand, B.
  • Aragnol, D.
  • Tolwinski, N. S.
  • Cole, M. D.
  • Pradel, J.
  • Yates III, John
  • Mishra, R. K.
  • Graba, Y.
  • Saurin, A. J.

publication date

  • March 2008

journal

  • EMBO Reports  Journal

abstract

  • Pontin (Pont) and Reptin (Rept) are paralogous ATPases that are evolutionarily conserved from yeast to human. They are recruited in multiprotein complexes that function in various aspects of DNA metabolism. They are essential for viability and have antagonistic roles in tissue growth, cell signalling and regulation of the tumour metastasis suppressor gene, KAI1, indicating that the balance of Pont and Rept regulates epigenetic programmes critical for development and cancer progression. Here, we describe Pont and Rept as antagonistic mediators of Drosophila Hox gene transcription, functioning with Polycomb group (PcG) and Trithorax group proteins to maintain correct patterns of expression. We show that Rept is a component of the PRC1 PcG complex, whereas Pont purifies with the Brahma complex. Furthermore, the enzymatic functions of Rept and Pont are indispensable for maintaining Hox gene expression states, highlighting the importance of these two antagonistic factors in transcriptional output.

subject areas

  • Animals
  • Carrier Proteins
  • Cell Cycle Proteins
  • Chromosomal Proteins, Non-Histone
  • DNA Helicases
  • Drosophila Proteins
  • Drosophila melanogaster
  • Gene Expression Regulation
  • Gene Silencing
  • Homeodomain Proteins
  • Mutation
  • Polycomb-Group Proteins
  • Protein Binding
  • Repressor Proteins
  • Trans-Activators
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Research

keywords

  • ATPase
  • Trithorax group
  • epigenetics
  • polycomb group
  • transcriptional regulation
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Identity

PubMed Central ID

  • PMC2267392

International Standard Serial Number (ISSN)

  • 1469-221X

Digital Object Identifier (DOI)

  • 10.1038/embor.2008.8

PubMed ID

  • 18259215
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Additional Document Info

start page

  • 260

end page

  • 266

volume

  • 9

issue

  • 3

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