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.