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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kim HY,Lee SB,Kang HS,Oh GT,Kim T

doi

10.1016/j.bbrc.2014.04.161

subject

Has Abstract

pub_date

2014-06-27 00:00:00

pages

202-7

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(14)00840-7

journal_volume

449

pub_type

杂志文章

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