By Sven Heinz, Christopher K. Glass (auth.), Cornelis Murre (eds.)

The reports defined during this quantity function a kick off point to familiarize one self with the multifarious adjustments in epigenetic designs that orchestrate the development of constructing blood cells. additionally they might function a basic paradigm for the mechanisms that underpin the regulate of eukaryotic gene expression.

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Nat Immunol 11:635–643 Lukin K, Fields S, Lopez D, Cherrier M, Ternyak K, Ramirez J, Feeney AJ, Hagman J (2010) Compound haploinsufficiencies of Ebf1 and Runx1 genes impede B cell lineage progression. Proc Natl Acad Sci USA 107:7869–7874 Lukin K, Fields S, Guerrettaz L, Straign D, Rodriguez V, Zandi S, Mansson R, Cambier JC, Sigvardsson M, Hagman J (2011) A dose-dependent role for EBF1 in repressing non-B-cellspecific genes. Eur J Immunol 41:1787–1793 Maier H, Colbert J, Fitzsimmons D, Clark DR, Hagman J (2003) Activation of the early B cellspecific mb-1 (Ig-a) gene by Pax-5 is dependent on an unmethylated Ets binding site.

2010b). These publications made use of ChIP-based technologies to assess the breadth of EBF1 binding to regulatory modules in the chromatin of pro-B cells. Common themes arising from these experiments included the extent of EBF1 DNA binding, which was detected at [500 genes. These sites were localized within sets of genes involved in a host of biological processes including pre-BCR, BCR and PI3K/Akt/ mTOR signaling, B cell adhesion, cell cycle control and migration. The studies also correlated EBF1 DNA binding with the status of epigenetic marks on histones.

2010a). The DNA sequence used for crystallization with EBF1 (including 50 -ATTCCCATGGGAAT-30 ) and the majority of EBF1 binding sites identified using ChIP and bioinformatics are highly palindromic. In contrast, the EBF1 binding site of the Cd79a promoters (50 -AGACTCAAGGGAAT-30 ) is less symmetric. Thus, the clamping mode of DNA binding may be critical for the ability of EBF1 to activate promoters with less than optimal binding sites. 3 Structures of Other Domains in EBF1 Regions of EBF1 involved in homodimerization were crystallized both as individual domains (Siponen et al.

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