A role for phosphorylated Pol II CTD in modulating transcription coupled histone dynamics
Marla M Spain1, Chhabi K Govind
1Department of Biological Sciences; Oakland University; Rochester, MI USA.
Abstract:
Histone acetylation modulates histone occupancy both at promoters and in coding sequences. Based on our recent observation that HDACs in the budding yeast, Saccharomyces cerevisiae, are co-transcriptionally recruited to coding regions by elongating polymerases, we propose a model in which Pol II facilitates recruitment of chromatin remodeling complexes as well as other factors required for productive elongation.
More Related Videos
11:02Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
Published on: May 17, 2016
10:59Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
Published on: May 13, 2019
Related Concept Videos
RNA Polymerase II Accessory Proteins
RNA Polymerase II Accessory Proteins
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Co-activators and Co-repressors
Histone Modification
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Histone Modification
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
