Related Experiment Video
Updated: Aug 13, 2026

Novel RNA-Binding Proteins Isolation by the RaPID Methodology
Published on: September 30, 2016
Interaction of a new polypeptide with yeast RNA polymerase B
Abstract:
A basic 37,000-dalton protein (P37), purified from yeast cells, interacts with yeast RNA polymerase B and drastically increases its specific activity. A complex of P37 and RNA polymerase can be isolated by sedimentation through a glycerol gradient. The complex is dissociated at the ionic strength of 0.9. The preferential binding of P37 with RNA polymerase form BI (with the unproteolyzed B220 subunit) was visualized by polyacrylamide gel electrophoresis under nondenaturing conditions. Kinetic analysis of the RNA polymerase cofactor interaction indicated that the dissociation constant for the complex is 5 X 10(-8) M.
More Related Videos
09:21Saccharomyces cerevisiae Metabolic Labeling with 4-thiouracil and the Quantification of Newly Synthesized mRNA As a Proxy for RNA Polymerase II Activity
Published on: October 22, 2018
07:31ACT1-CUP1 Assays Determine the Substrate-Specific Sensitivities of Spliceosomal Mutants in Budding Yeast
Published on: June 30, 2022
Related Concept Videos
Yeast Signaling
Bacterial RNA Polymerase
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
Eukaryotic RNA Polymerases
All three eukaryotic RNAPs require specific transcription factors, of which the...
Transcription Initiation
The promoters and enhancers and their accessory proteins allow tight regulation of...
Bacterial RNA Polymerase
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
Eukaryotic RNA Polymerases
All three eukaryotic RNAPs require specific transcription factors, of which the...