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Related Concept Videos

General Transcription Factors01:30

General Transcription Factors

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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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The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
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The basic structure of RNA consists of a five-carbon sugar and one of four nitrogenous bases. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
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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.
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One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
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Transcription elongation is a dynamic process that alters depending upon the sequence heterogeneity of the DNA being transcribed. Hence, it is not surprising that the elongation complex's composition also varies along the way while transcribing a gene.
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Updated: Dec 22, 2025

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
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eIF4G has intrinsic G-quadruplex binding activity that is required for tiRNA function.

Shawn M Lyons1,2,3,4, Prakash Kharel1,2, Yasutoshi Akiyama1,2,5

  • 1Division of Rheumatology, Inflammation and Immunity, Brigham and Women's Hospital, Boston, MA, USA.

Nucleic Acids Research
|May 7, 2020
PubMed
Summary
This summary is machine-generated.

Small RNAs called tiRNAs, especially those forming G-quadruplex (G4) structures, inhibit cell translation. This study reveals tiRNAs target eIF4G, a key protein, to block translation initiation and mRNA scanning.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • RNA Biology

Background:

  • Cellular stress responses, including translation inhibition, protect cells from adverse conditions like hypoxia and nutrient deprivation.
  • tRNA-derived small RNAs (tiRNAs) are increasingly recognized for their role in regulating stress responses.
  • G-quadruplex (G4) forming tiRNAs are potent regulators, but their mechanism of translation inhibition remains unclear.

Purpose of the Study:

  • To elucidate the mechanism by which tiRNAs, particularly G4-forming tiRNAs, inhibit protein translation.
  • To identify the direct molecular targets of tiRNAs involved in translation repression.
  • To understand the role of the translation initiation complex scaffolding protein eIF4G in tiRNA-mediated regulation.

Main Methods:

  • Investigated the interaction between G4 structures and the translation initiation factor eIF4G.
  • Assessed the requirement of eIF4G binding for tiRNA-mediated translation repression.
  • Analyzed the impact of targeting eIF4G on ribosome scanning and stress granule formation.

Main Results:

  • Demonstrated that eIF4G directly binds to G4 structures formed by tiRNAs.
  • Showed that this eIF4G binding activity is essential for tiRNA-mediated translation repression.
  • Revealed that targeting eIF4G impairs 40S ribosome scanning on messenger RNAs (mRNAs).
  • Observed the formation of eIF2α-independent stress granules upon eIF4G targeting.

Conclusions:

  • Elucidated the mechanism of tiRNA-mediated translation inhibition, involving direct binding of tiRNAs to eIF4G.
  • Identified a novel regulatory role for eIF4G in controlling translation initiation and mRNA scanning.
  • Established that tiRNA targeting of eIF4G leads to impaired ribosome function and stress granule assembly.