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Hatano, N., Itoh, Y., Suzuki, H., Muraki, Y., Hayashi, H., Onozaki, K., Wood, I.C., Beech, D.J. and Muraki, K. (2012) Hypoxia-inducible factor-1α (HIF1α) switches on transient receptor potential ankyrin repeat 1 (TRPA1) gene expression via a hypoxia response element-like Motif to modulate cytokine release. Journal of Biological Chemistry, 287, 31962-31972. doi:10.1074/jbc.M112.361139

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• TITLE: Shared and discrete interacting partners of ELL1 and ELL2 by yeast two-hybrid assay

  AUTHORS: Fortuna Arumemi, Ian Bayles, Joshua Paul, Christine Milcarek

  KEYWORDS: Transcription Elongation; Immunoglobulin Synthesis; Yeast Two-Hybrid System

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.4 No.7, July 3, 2013

  ABSTRACT: ELL2 (eleven-nineteen lysine-rich leukemia transcription elongation factor), a component of a larger complex with pTEFb (cyclin T and CDK9) and AF4, is up-regulated in plasma cells where it influences mRNA processing by increasing exon skipping and enhancing proximal poly (A) site use. ELL2 is needed to produce the secretory-specific Ig heavy chain mRNA while ELL1 mRNA does not change in abundance with B cell stages. To investigate the potential interactions of other proteins with the ELL1 and ELL2 proteins, we preformed yeast two-hybrid studies. HSP40 and Testin were found to bind to ELL2 in its amino-terminal half. PCNA binds to ELL2 in a region encompassing amino acids 186 - 344. The potent transcription factors HIF1 α and ZNF622 interact with both ELL1 and 2 in the central, proline rich region. Meanwhile, BBS2 and ING3 interact with ELL1 but not ELL2 in this central proline-rich region. Many of the ELL-interacting-proteins uncovered in the two-hybrid screen are tumour suppressors that may work through the ELL: pTEFb complex to suppress or activate sets of genes in plasma cells.