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Related Concept Videos

Eukaryotic Transcription Inhibitors01:52

Eukaryotic Transcription Inhibitors

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Certain biochemical processes, such as embryonic development and cell growth regulation, depend on the repression of specific genes. DNA binding proteins known as eukaryotic transcription inhibitors regulate the repression of gene expression in eukaryotes. The presence of these inhibitors at the required location and time in the cell is triggered by the presence of hormones and additional signals from other cells.
Eukaryotic transcription inhibitors usually contain two distinct domains, a...
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General Transcription Factors01:30

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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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Initiation of Translation02:33

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Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
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Transcription Initiation01:47

Transcription Initiation

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Initiation is the first step of transcription in eukaryotes. Prokaryotic RNA Polymerase (RNAP) can bind to the template DNA and start transcribing. On the other hand, transcription in eukaryotes requires additional proteins, called transcription factors, to first bind to the promoter region in the DNA template. This binding helps recruit the specific RNAP that can assemble on the DNA and start transcription.
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Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

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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.
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Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
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Eukaryotic initiation factor 4B and the poly(A)-binding protein bind eIF4G competitively.

Shijun Cheng1, Daniel R Gallie1

  • 1Department of Biochemistry; University of California; Riverside, CA USA.

Translation (Austin, Tex.)
|January 30, 2016
PubMed
Summary

Plant eukaryotic translation initiation factor (eIF) 4G has distinct binding sites for poly(A) binding protein (PABP) and eIF4B, which compete for binding. This competitive binding occurs at two sites on eIF4G, differing from eIFiso4G interactions.

Keywords:
eIF4AeIF4BeIF4Gpoly(A) binding proteinprotein synthesistranslation initiation

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Area of Science:

  • Molecular Biology
  • Plant Science
  • Protein Interactions

Background:

  • Eukaryotic translation initiation factor (eIF) 4G is crucial for assembling the translation initiation complex.
  • Plants possess two divergent eIF4G isoforms: eIF4G and eIFiso4G.
  • The domain organization of plant eIF4G is largely uncharacterized compared to other eukaryotes.

Purpose of the Study:

  • To investigate the domain organization and protein interaction sites of plant eIF4G.
  • To compare the binding properties of eIF4G with its isoform, eIFiso4G.
  • To elucidate the competitive binding mechanisms between poly(A) binding protein (PABP), eIF4B, and eIF4A with eIF4G.

Main Methods:

  • Analysis of protein domain organization.
  • Mapping of protein-protein interaction domains.
  • Competitive binding assays to study interactions between eIF4G, eIFiso4G, PABP, eIF4B, and eIF4A.

Main Results:

  • Plant eIF4G contains two distinct interaction domains for PABP and eIF4B, unlike eIFiso4G.
  • Both PABP and eIF4B bind competitively to the same N-terminal region and a middle domain region of eIF4G.
  • Unlike eIFiso4G, eIF4G does not exhibit competitive binding between PABP/eIF4B and eIF4A at its HEAT-1 domain.

Conclusions:

  • Plant eIF4G exhibits unique domain organization and binding characteristics compared to eIFiso4G.
  • Competitive binding between PABP and eIF4B is a key feature of eIF4G function.
  • Despite sequence and structural divergence, conserved competitive binding principles exist for PABP and eIF4B across eIF4G isoforms.