Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme.

Ets transcription factors have Ets DNA binding domains, that have a winged helix-turn-helix structure. ETS-1, the founding member of the family, is regulated by the Ras and Ca2+ signaling pathways and is implicated in various physiological processes leading to cell growth, differentiation and apoptosis. We have identified ETS-1 interacting factors ...
with a yeast two-hybrid screen. The majority of the positive clones turned out to encode the human homologue of the yeast ubiquitin-conjugating enzymes UBC9 and Hus5. In two different yeast assays, ETS-1 interacted with huUBC9. In an in vitro GST 'pull-down' assay, ETS-1 and several other Ets family members complexed with huUBC9. Interestingly, in mammalian cells, coexpression of huUBC9 resulted in a substantial increase in the transcriptional activity of ETS-1. Coexpressed huUBC9 did not affect the ETS-1 protein level, and moreover, a point mutation at Cys93, an amino acid known to be essential for ubiquitination, did not abolish the stimulation of the ETS-1 transcriptional activity. Our results indicate that the modulation of ETS-1 activity by huUBC9 results from processes other than ubiquitination and ETS-1 stabilization.
Mesh Terms:
Amino Acid Sequence, Base Sequence, Binding Sites, Cloning, Molecular, Humans, Ligases, Molecular Sequence Data, Protein-Tyrosine Kinases, Proto-Oncogene Protein c-ets-1, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-ets, Recombinant Fusion Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Transcription Factors, Transcription, Genetic, Ubiquitin-Conjugating Enzymes
Oncogene
Date: Sep. 18, 1997
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