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Related Concept Videos

Transfer RNA Synthesis02:36

Transfer RNA Synthesis

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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.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
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Tail-anchoring of Proteins in the ER Membrane01:45

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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tRNA Activation02:26

tRNA Activation

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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
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Leaky Scanning02:28

Leaky Scanning

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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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RNA Structure01:19

RNA Structure

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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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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.
All three eukaryotic RNAPs require specific transcription factors, of which the...
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Related Experiment Video

Updated: Jun 8, 2025

Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro
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Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro

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Structural insights into human ELAC2 as a tRNA 3' processing enzyme.

Chenyang Xue1,2, Junshan Tian1,2, Yanhong Chen3

  • 1Shenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology, Shenzhen 518055 Guangdong, China.

Nucleic Acids Research
|November 4, 2024
PubMed
Summary

Human elaC ribonuclease Z 2 (ELAC2) enzyme

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Human elaC ribonuclease Z 2 (ELAC2) is crucial for precursor transfer ribonucleic acid (pre-tRNA) processing.
  • Mutations in ELAC2 are linked to prostate cancer and hypertrophic cardiomyopathy.
  • The catalytic mechanism of ELAC2 remains poorly understood.

Purpose of the Study:

  • To elucidate the structural basis of ELAC2's pre-tRNA binding and cleavage activity.
  • To understand the role of ELAC2 structure in disease-associated mutations.

Main Methods:

  • Cryogenic electron microscopy (cryo-EM) to determine structures of human ELAC2 in apo, pre-tRNA-bound, and tRNA-bound states.
  • Biochemical assays to analyze the impact of disease-related mutations.

Main Results:

  • Detailed structures reveal how ELAC2 binds pre-tRNA via its flexible arm domain.
  • Conformational changes, particularly in the C-terminal helix, facilitate 3' trailer feeding into the active site.
  • Structural effects of disease-associated mutations were characterized.

Conclusions:

  • The study provides a comprehensive structural understanding of ELAC2's mechanism in pre-tRNA processing.
  • The findings offer insights into how ELAC2 mutations contribute to disease development.
  • This work lays the foundation for future therapeutic strategies targeting ELAC2.