2000
DOI: 10.1073/pnas.140109897
|View full text |Cite
|
Sign up to set email alerts
|

A regulatory shortcut between the Snf1 protein kinase and RNA polymerase II holoenzyme

Abstract: RNA polymerase II holoenzymes respond to activators and repressors that are regulated by signaling pathways. Here we present evidence for a ''shortcut'' mechanism in which the Snf1 protein kinase of the glucose signaling pathway directly regulates transcription by the yeast holoenzyme. In response to glucose limitation, the Snf1 kinase stimulates transcription by holoenzyme that has been artificially recruited to a reporter by a LexA fusion to a holoenzyme component. We show that Snf1 interacts physically with… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

7
113
0
1

Year Published

2001
2001
2019
2019

Publication Types

Select...
6
3

Relationship

1
8

Authors

Journals

citations
Cited by 101 publications
(121 citation statements)
references
References 40 publications
7
113
0
1
Order By: Relevance
“…Plasmid p35mLuc containing 35S mp-Luc was used as a control reporter, and the Ubi-SnRK1A construct was used as the effector. SnRK1A activated the CaMV35S minimal promoter fourfold (Figure 3), regardless of the presence or absence of glucose, likely due to a general chromatin-remodeling activity of SnRK1A for many promoters, as has been reported for the yeast Snf1 (Kuchin et al, 2000;Lo et al, 2005). In the absence of SnRK1A overexpression, luciferase activities were low for all constructs, except for the wild-type SRC, which was induced by glucose starvation (Figure 3).…”
Section: Snrk1amentioning
confidence: 57%
“…Plasmid p35mLuc containing 35S mp-Luc was used as a control reporter, and the Ubi-SnRK1A construct was used as the effector. SnRK1A activated the CaMV35S minimal promoter fourfold (Figure 3), regardless of the presence or absence of glucose, likely due to a general chromatin-remodeling activity of SnRK1A for many promoters, as has been reported for the yeast Snf1 (Kuchin et al, 2000;Lo et al, 2005). In the absence of SnRK1A overexpression, luciferase activities were low for all constructs, except for the wild-type SRC, which was induced by glucose starvation (Figure 3).…”
Section: Snrk1amentioning
confidence: 57%
“…Although Gts1p is a phosphorylated protein (25), it is unlikely that Gts1p is a phosphorylation target of Snf1 kinase, because it does not have any sequence motifs for the kinase. Rather, because Gts1p was shown to bind to Snf1 kinase by our affinity precipitation analysis, we suggest that Gts1p functions as one of transcriptional modulators for Snf1 kinase, which then functions in the RNA polymerase II holoenzyme complex (46). Alternatively, because Snf1 kinase has been recognized as a component of a histone kinase complex that works in concert with the histone acetyltransferase Gcn5 (47), it is possible that Gts1p regulates transcription by controlling histone modification via interaction with Snf1 kinase.…”
Section: Discussionmentioning
confidence: 88%
“…Snf1 regulates transcription in numerous ways, including transcription factor activation and inactivation (14 -19), modification of chromatin (20 -22), and perhaps by acting directly on the transcription apparatus (23). Snf1 also has a role in posttranscriptional regulation of gene expression.…”
mentioning
confidence: 99%