Two distinct domains of Flo8 activator mediates its role in transcriptional activation and the physical interaction with Mss11

Hye Young Kim, Sung Bae Lee, Hyen Sam Kang, Goo Taeg Oh, Taesoo Kim

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

Flo8 is a transcriptional activator essential for the inducible expression of a set of target genes such as STA1, FLO11, and FLO1 encoding an extracellular glucoamylase and two cell surface proteins, respectively. However, the molecular mechanism of Flo8-mediated transcriptional activation remains largely elusive. By generating serial deletion constructs, we revealed here that a novel transcriptional activation domain on its extreme C-terminal region plays a crucial role in activating transcription. On the other hand, the N-terminal LisH motif of Flo8 appears to be required for its physical interaction with another transcriptional activator, Mss11, for their cooperative transcriptional regulation of the shared targets. Additionally, GST pull-down experiments uncovered that Flo8 and Mss11 can directly form either a heterodimer or a homodimer capable of binding to DNA, and we also showed that this formed complex of two activators interacts functionally and physically with the Swi/Snf complex. Collectively, our findings provide valuable clues for understanding the molecular mechanism of Flo8-mediated transcriptional control of multiple targets.

Original languageEnglish
Pages (from-to)202-207
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume449
Issue number2
DOIs
StatePublished - 27 Jun 2014

Keywords

  • FLO1
  • FLO11
  • Flo8
  • LisH motif
  • Mss11
  • Transcriptional activation

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