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Related Concept Videos

Improving Translational Accuracy02:07

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
Initiation of Translation02:33

Initiation of Translation

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.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
Initiation of Translation02:33

Initiation of Translation

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.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
Transcription Elongation Factors02:35

Transcription Elongation Factors

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.
The transcription elongation is regulated via pausing of RNA polymerase on several occasions during transcription. In bacteria, these halts are necessary because the transcription of DNA into mRNA is coupled to the translation of that mRNA into a...
Transcription Elongation Factors02:35

Transcription Elongation Factors

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.
The transcription elongation is regulated via pausing of RNA polymerase on several occasions during transcription. In bacteria, these halts are necessary because the transcription of DNA into mRNA is coupled to the translation of that mRNA into a...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...

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Related Experiment Video

Updated: Jul 16, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

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Published on: May 1, 2020

HDM2-binding partners: interaction with translation elongation factor EF1alpha.

Rebecca Frum1, Scott A Busby, Mahesh Ramamoorthy

  • 1Department of Biochemistry and the Massey Cancer Center, Virginia Commonwealth University, Richmond, Virginia 23298, USA.

Journal of Proteome Research
|March 22, 2007
PubMed
Summary

This study identifies new proteins interacting with HDM2, including translation factor EF1alpha, independent of p53. This discovery suggests a novel role for HDM2 in cell growth regulation.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Oncology

Background:

  • HDM2 is a key regulator of the tumor suppressor p53.
  • Understanding HDM2's cellular functions beyond p53 is crucial for cancer research.

Purpose of the Study:

  • To identify novel HDM2-interacting proteins.
  • To investigate the functional significance of HDM2 interactions, particularly in a p53-independent manner.

Main Methods:

  • Proteomic analysis to identify interacting proteins.
  • Immunoprecipitation and Western blot to confirm interactions.
  • Colocalization studies to assess protein localization.

Main Results:

  • HDM2 interacts with translation elongation factor EF1alpha, ribosomal protein S20, tubulins, and glyceraldehyde 3-phosphate dehydrogenase.
  • HDM2 and EF1alpha interaction is confirmed in various cell types and observed in cancer cells overexpressing HDM2.
  • Specific HDM2 domains (1-58 and 221-325) are essential for EF1alpha binding, independent of p53-related ribosomal proteins.

Conclusions:

  • HDM2 interacts with EF1alpha, suggesting a p53-independent role in cell growth regulation.
  • The interaction between HDM2 and EF1alpha may be involved in oncogenesis and cellular processes like DNA replication or microtubule dynamics.