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Related Concept Videos

Eukaryotic Transcription Activators02:42

Eukaryotic Transcription Activators

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Transcription activators are proteins that promote the transcription of genes from DNA to RNA. In most cases, these proteins contain two separate domains ‒ a domain that binds to DNA and a domain for activating transcription; however, in some cases, a single domain is responsible for both binding and activation of transcription, as seen in the glucocorticoid receptor and MyoD.
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Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
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RNA Polymerase II Accessory Proteins02:36

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Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
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Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
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Related Experiment Video

Updated: Apr 1, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
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EBNA2 and Its Coactivator EBNA-LP.

Bettina Kempkes1, Paul D Ling2

  • 1Department of Gene Vectors, Helmholtz Center Munich, German Research Center for Environmental Health, Marchioninistr. 25, 81377, Munich, Germany. kempkes@helmholtz-muenchen.de.

Current Topics in Microbiology and Immunology
|October 3, 2015
PubMed
Summary
This summary is machine-generated.

Epstein-Barr virus (EBV) uses distinct latent programs for B-cell growth. This review focuses on how EBNA2 and EBNA-LP proteins drive EBV-mediated B-cell transformation during latency III.

Keywords:
CBF1EBNA2EBNA‐LPTarget genesTransactivation

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Area of Science:

  • Virology
  • Immunology
  • Molecular Biology

Background:

  • Epstein-Barr virus (EBV) establishes lifelong infections by alternating between lytic and latent cycles.
  • Latent EBV infection is characterized by distinct viral transcription programs: latency I, II, and III.
  • B-cell growth transformation by EBV in vitro involves Epstein-Barr virus nuclear antigens (EBNAs) and latent membrane proteins (LMPs).

Purpose of the Study:

  • To review the current understanding of EBV latency III.
  • To elucidate the roles of EBNA2 and EBNA-LP in EBV-mediated B-cell growth transformation.

Main Methods:

  • Review of existing literature on EBV latency programs.
  • Analysis of the functions of EBNA2 and EBNA-LP in B-cell transformation.

Main Results:

  • Latency III is characterized by the coexpression of multiple EBNAs (EBNA1, EBNA2, EBNA-LP, EBNA3A, -3B, -3C) and LMPs (LMP1, LMP2A, LMP2B).
  • EBNA2 and EBNA-LP are key drivers of EBV-mediated B-cell growth transformation.

Conclusions:

  • EBNA2 and EBNA-LP play critical roles in the EBV latency III program.
  • Understanding these proteins' functions is crucial for comprehending EBV's impact on B-cells.