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Related Concept Videos

Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
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 Polymerases00:58

Eukaryotic RNA Polymerases

RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...
Bacterial Transcription01:53

Bacterial Transcription

RNA polymerase (RNAP) carries out DNA-dependent RNA synthesis in both bacteria and eukaryotes. Bacteria do not have a membrane-bound nucleus. So, transcription and translation occur simultaneously, on the same DNA template.
Transcription can be divided into three main stages, each involving distinct DNA sequences to guide the polymerase. These are:
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
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 Polymerases00:58

Eukaryotic RNA Polymerases

RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...
General Transcription Factors01:30

General Transcription Factors

Tissue-specific transcription factors contribute to diverse cellular functions in mammals. For example, the gene for beta globin, a major component of hemoglobin, is present in all cells of the body. However, it is only expressed in red blood cells because the transcription factors that can bind to the promoter sequences of the beta globin gene are only expressed in these cells. Tissue-specific transcription factors also ensure that mutations in these factors may impair only the function of...

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Transcription factor TFIIIB and transcription by RNA polymerase III.

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The protein kinase Pho85 is required for asymmetric accumulation of the Ash1 protein in Saccharomyces cerevisiae.

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The Swi5 activator recruits the Mediator complex to the HO promoter without RNA polymerase II.

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Related Experiment Video

Updated: Jun 23, 2026

High-throughput Purification of Affinity-tagged Recombinant Proteins
07:44

High-throughput Purification of Affinity-tagged Recombinant Proteins

Published on: August 26, 2012

Effects of temperature and single-stranded DNA on the interaction of an RNA polymerase III transcription factor with

D J Stillman, P Caspers, E P Geiduschek

    Cell
    |February 1, 1985
    PubMed
    Summary

    A yeast transcription factor stably binds to tRNA genes, with key DNA contacts mapped to promoter regions. This binding exhibits properties similar to prokaryotic systems, with stability increasing at higher temperatures.

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    Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

    Published on: May 13, 2019

    Area of Science:

    • Molecular Biology
    • Genetics
    • Biochemistry

    Background:

    • Yeast RNA polymerase III transcription factors are known to bind tRNA genes.
    • Understanding protein-DNA interactions is crucial for gene regulation.

    Purpose of the Study:

    • To map the principal protein-DNA contacts of a yeast RNA polymerase III transcription factor on a tRNA gene.
    • To investigate the influence of DNA structure and temperature on transcription factor binding.

    Main Methods:

    • Dimethylsulfate footprinting was used to identify protein-DNA contact sites.
    • Single-stranded DNA interference assays were performed.
    • The effect of temperature on complex formation was analyzed.

    Main Results:

    • Principal protein-DNA contacts were localized to the A and B block promoter regions of the S. cerevisiae tRNALeu3 gene.
    • Single-stranded DNA preferentially disrupted binding to one promoter region.
    • The transcription factor-DNA complex displayed an "opening" property, with increased stability at higher temperatures.

    Conclusions:

    • The study precisely mapped critical interactions between a yeast transcription factor and tRNA gene promoters.
    • The findings reveal insights into the dynamic nature of transcription factor binding, influenced by DNA structure and temperature.