Volume 6 Supplement 1

Epigenetics and Chromatin: Interactions and processes

Open Access

Set1 cooperates with CENP-B in genome organization and transcriptome regulation

  • David R Lorenz1,
  • Irina V Mikheyeva1,
  • Lauren Meyer1,
  • Peter Johansen1,
  • Anastasia Berg1,
  • Shiv IS Grewal2 and
  • Hugh P Cam1
Epigenetics & Chromatin20136(Suppl 1):P12


Published: 18 March 2013

Chromatin modifiers impose regulatory controls over diverse chromosomal processes including transcription, nuclear organization, and genome stability. Here we reveal an unexpected role for the histone methyltransferase Set1 (KMT2) as a general transcriptional repressor of the fission yeast Schizosaccharomyces pombe genome. Set1 localizes to repetitive elements and represses both forward and reverse transcripts associated with centromeric and subtelomeric heterochromatin and Tf2 long terminal repeats (LTRs) retrotransposons distinct from its H3K4 methylation (H3K4me) activity. Set1 cooperates with Abp1, the S. pombe homolog of the mammalian centromere binding protein B (CENP-B), to mediate its repression of Tf2s. Intriguingly, Set1 helps organize dispersed Tf2s into distinct nuclear foci termed Tf bodies, the integrity of which requires class I/II histone deacetylases (HDACs) and Sirtuin. Our study uncovers dual roles for Set1 in the maintenance of euchromatin and heterochromatin, and its cooperation with a functional transposase-containing transcription factor to mediate repression and genome organization of dispersed retrotransposons.

Authors’ Affiliations

Biology Department Chestnut Hill, Boston College
Laboratory of Biochemistry and Molecular Biology National Cancer Institute, National Institutes of Health


© Lorenz et al; licensee BioMed Central Ltd. 2013

This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.