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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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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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Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

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Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
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Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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Phase II Reactions: Miscellaneous Conjugation Reactions01:19

Phase II Reactions: Miscellaneous Conjugation Reactions

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Phase II biotransformations are detoxification mechanisms that conjugate xenobiotics with endogenous substances, neutralizing their toxicity.
A key example involves the conjugation of cyanide ions, which impair cellular respiration and alter hemoglobin into non-oxygen-carrying cyanmethemoglobin. To neutralize this threat, a sulfur atom from thiosulphate is transferred to the cyanide ion, catalyzed by the enzyme rhodanese, resulting in an inactive compound called thiocyanate. The production of...
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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
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[4Fe-4S]-dependent enzymes in non-redox tRNA thiolation.

Sylvain Gervason1, Sambuddha Sen1, Marc Fontecave1

  • 1Laboratoire de Chimie des Processus Biologiques, UMR 8229 CNRS, Collège de France, Sorbonne Université, 11 Place Marcelin Berthelot, 75231, Paris cedex 05, France.

Biochimica Et Biophysica Acta. Molecular Cell Research
|August 6, 2024
PubMed
Summary

Transfer RNA (tRNA) thiolation, crucial for protein synthesis, is increasingly understood to involve [4Fe-4S] clusters. This review details the biochemical and structural insights into these non-redox tRNA thiolation enzymes.

Keywords:
FeS clusterIron-sulfur clusterNon-redox reactionSulfurationThiolationtRNA modification

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Post-transcriptional modification of nucleosides in transfer RNAs (tRNAs) is essential for accurate protein synthesis.
  • Sulfur-containing nucleosides like 2-thiouridine (s²U) and 2-methylthioadenosine (ms²A) are vital modifications within tRNAs.
  • While persulfide chemistry was the long-standing model, [4Fe-4S] clusters are now recognized in many tRNA thiolation enzymes.

Purpose of the Study:

  • To review recent advancements in understanding [4Fe-4S]-dependent tRNA thiolation enzymes.
  • To summarize biochemical, spectroscopic, and structural data on these enzymes.
  • To highlight the shift from persulfide chemistry to [4Fe-4S] cluster involvement in tRNA thiolation.

Main Methods:

  • Biochemical characterization of tRNA thiolation enzymes.
  • Spectroscopic analyses to study enzyme mechanisms and structures.
  • X-ray crystallography and other structural biology techniques to determine enzyme structures.

Main Results:

  • Multiple tRNA thiolation enzymes utilize [4Fe-4S] clusters for their catalytic activity.
  • Detailed biochemical and structural data reveal the mechanisms of these novel enzymes.
  • The role of [4Fe-4S] clusters in non-redox tRNA thiolation is elucidated.

Conclusions:

  • [4Fe-4S] clusters are a key feature of many tRNA thiolation enzymes, representing a significant departure from previous models.
  • Understanding these enzymes is crucial for comprehending the fidelity of translation.
  • This review consolidates a decade of research on these important biological catalysts.