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

Autor:	Christine Milcarek, Ian Bayles, Joshua Paul, Fortuna Arumemi
Rok vydání:	2013
Předmět:	chemistry.chemical_classification Messenger RNA Two-hybrid screening General Medicine Biology Molecular biology Exon skipping Cell biology Amino acid Testin chemistry Cyclin-dependent kinase 9 Transcription factor Gene
Zdroj:	Advances in Bioscience and Biotechnology. :774-780
ISSN:	2156-8502 2156-8456
DOI:	10.4236/abb.2013.47101
Popis:	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.
Databáze:	OpenAIRE
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