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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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RNA Editing02:23

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RNA editing is a post-transcriptional modification where a precursor mRNA (pre-mRNA) nucleotide sequence is changed by base insertion, deletion, or modification. The extent of RNA editing varies from a few hundred bases, in mitochondrial DNA of trypanosomes, to a just single base, in nuclear genes of mammals. Even a single base change in the pre-mRNA can convert a codon for one amino acid into the codon for another amino acid or a stop codon. This type of re-coding can significantly affect the...
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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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Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
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An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity
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The Evolution of Substrate Specificity by tRNA Modification Enzymes.

Katherine M McKenney1, Mary Anne T Rubio1, Juan D Alfonzo1

  • 1Department of Microbiology, Ohio State Biochemistry Program, The Center for RNA Biology, The Ohio State University, Columbus, OH, United States.

The Enzymes
|June 12, 2017
PubMed
Summary

Cellular nucleic acids, especially transfer RNA (tRNA), undergo numerous chemical modifications crucial for function. Understanding how tRNA modification enzymes recognize their substrates is key to deciphering RNA biology.

Keywords:
EditingMethylationPseudouridineRNA binding

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Cells utilize diverse chemical modifications on nucleic acids, including DNA and various RNAs like tRNA, mRNA, and rRNA.
  • Over 100 distinct modifications exist, affecting bases and sugars, with significant implications for RNA structure and function.
  • The evolutionary conservation and genomic investment in modification enzymes underscore the importance of these post-transcriptional changes.

Purpose of the Study:

  • To investigate the molecular mechanisms of substrate recognition by tRNA modification enzymes.
  • To explore general principles of RNA binding relevant to the broader field of RNA modification.

Main Methods:

  • Focus on well-characterized tRNA modification enzymes.
  • Analysis of specific examples to understand RNA-binding modes.
  • Drawing generalizable conclusions from detailed case studies.

Main Results:

  • Detailed understanding of RNA binding is central to tRNA modification.
  • Specific enzymes exhibit diverse strategies for substrate recognition.
  • Identified common themes in RNA-enzyme interactions across different modification pathways.

Conclusions:

  • Elucidating enzyme-substrate interactions is critical for understanding tRNA modification.
  • Generalizable principles of RNA binding can be derived from studying individual modification enzymes.
  • This work provides insights applicable to the broader field of RNA modification and its enzymes.