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Two distinct domains of Flo8 activator mediates its role in transcriptional activation and the physical interaction with Mss11
- Two distinct domains of Flo8 activator mediates its role in transcriptional activation and the physical interaction with Mss11
- Kim, HY[Kim, Hye Young]; Lee, SB[Lee, Sung Bae]; Kang, HS[Kang, Hyen Sam]; Oh, GT[Oh, Goo Taeg]; Kim, T[Kim, TaeSoo]
- DGIST Authors
- Lee, SB[Lee, Sung Bae]
- Issue Date
- Biochemical and Biophysical Research Communications, 449(2), 202-207
- Article Type
- Amino Terminal Sequence; Cell Surface Protein; DNA-Binding; FLO1; FLO11; Flo8; FLO8 Gene; Fungal Gene; Fungal Protein; Gene; Gene Deletion; Gene Expression Regulation, Fungal; Gene Targeting; Genes, Fungal; Glucan 1,4 Alpha Glucosidase; Heterodimer; Homodimer; Lish Motif; Mannose-Binding Lectins; Membrane Glycoproteins; Mss11; Mss11 Protein; Multiprotein Complexes; Non-Human; Nuclear Proteins; Priority Journal; Protein Domain; Protein Interaction Domains and Motifs; Protein Motif; Recombinant Fusion Proteins; Saccharomyces Cerevisiae; Saccharomyces Cerevisiae Proteins; Trans-Activators; Transcription Factors; Transcription Initiation; Transcriptional Activation; Unclassified Drug
- 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. © 2014 Elsevier Inc. All rights reserved.
- Academic Press Inc.
- Related Researcher
Lee, Sung Bae
SB LAB(Lab of Neurodegenerative diseases and Aging)
Cellular mechanism of neurodegenerative diseases; Neuronal maintenance and remodeling; 퇴행성 뇌질환의 세포기전; 신경계 유지 및 리모델링 연구
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