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Du, J.X., Hagos, E.G., Nandan, M.O., Bialkowska, A.B., Yu, B. and Yang, V.W. (2011) The E3 ubiquitin ligase SMAD ubiquitination regulatory factor 2 negatively regulates Krüppel-like factor 5 protein. Journal of Biological Chemistry, 286, 40354-40364. doi:10.1074/jbc.M111.258707

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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.