E-MTAB-1253 - Myb-domain protein Teb1 controls histone levels and centromere assembly in fission yeast
Released on 14 August 2013, last updated on 3 June 2014
The TTAGGG motif is common to two seemingly unrelated dimensions of chromatin function – the vertebrate telomere repeat and the promoter regions of many Schizosaccharomyces pombe genes, including all of those encoding canonical histones. The essential S. pombe protein Teb1 contains two Myb-like DNA binding domains related to those found in telomere proteins and binds the human telomere repeat sequence TTAGGG. Here we analyze Teb1 binding throughout the genome and the consequences of reduced Teb1 function. ChIP on chip analysis reveals robust Teb1 binding at many promoters, notably including all of those controlling canonical histone gene expression. A hypomorphic allele, teb1-1, confers reduced binding and reduced levels of histone transcripts. teb1-1 cells also show severe defects in the G1-arrest-associated clipping of histones, most likely due to a role for Teb1 in promoting expression of the protease Isp6. Prompted by previously suggested connections between histone expression and centromere identity, we examined localization of the centromeric histone H3 variant Cnp1 and found reduced centromeric binding along with reduced centromeric silencing. These data identify Teb1 as a master regulator of histone levels and centromere identity.
ChIP-chip by array, co-expression, growth condition, replicate
Myb-domain protein Teb1 controls histone levels and centromere assembly in fission yeast. Valente LP, Dehé PM, Klutstein M, Aligianni S, Watt S, Bähler J, Cooper JP. :450-460 (2013), PMID:23314747
Myb-domain protein Teb1 controls histone levels and centromere assembly in fission yeast. luis P. Valente, Pierre-Marie Dehe, Michael Klutstein, Sofia Aligianni, Stephen Watt, Jürg Bähler, Julia Promisel Cooper. , PMID:23314747