Phosphorylation of the Gal4 DNA-binding domain is essential for activator mono-ubiquitylation and efficient promoter occupancy-Reference-Cited by-同舟云学术

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Phosphorylation of the Gal4 DNA-binding domain is essential for activator mono-ubiquitylation and efficient promoter occupancy

Published:2008 Issue:11 Volume:4 Page:1116
ISSN:1742-206X
Container-title:Molecular BioSystems
language:en
Short-container-title:Mol. BioSyst.

Author:

Ferdous Anwarul,O’Neal Melissa,Nalley Kip,Sikder Devanjan,Kodadek Thomas,Johnston Stephen Albert

Publisher

Royal Society of Chemistry (RSC)

Subject

Molecular Biology,Biotechnology

Link

http://pubs.rsc.org/en/content/articlepdf/2008/MB/B809291E

Reference55 articles.

1. The Cell as a Collection of Protein Machines: Preparing the Next Generation of Molecular Biologists

2. Mutations in TFIIIA That Increase Stability of the TFIIIA-5 S rRNA Gene Complex

3. Dissociation Time from DNA Determines Transcriptional Function in a STAT1 Linker Mutant

4. The role of the proteasomal ATPases and activator monoubiquitylation in regulating Gal4 binding to promoters

5. Activation Domain-dependent Monoubiquitylation of Gal4 Protein Is Essential for Promoter Binding in Vivo

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1. Massively parallel single-amino-acid mutagenesis;Nature Methods;2015-01-05

2. Solvent-exposed serines in the Gal4 DNA-binding domain are required for promoter occupancy and transcriptional activationin vivo;FEMS Yeast Research;2013-10-25

3. Regulation of gene expression by the ubiquitin-proteasome system;Seminars in Cell & Developmental Biology;2012-07

4. Weak Organic Acid Stress Triggers Hyperphosphorylation of the Yeast Zinc-Finger Transcription Factor War1 and Dampens Stress Adaptation;OMICS: A Journal of Integrative Biology;2010-10

5. Phosphorylation within the MafA N Terminus Regulates C-terminal Dimerization and DNA Binding;Journal of Biological Chemistry;2010-04

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