Related Experiment Video

Updated: Jul 19, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Origins of the aminoglycoside modifying enzymes

P N Rather1

  • 1Department of Medicine, Case Western Reserve University, Cleveland, Ohio 44106, USA. pxr17@po.cwru.edu

Drug Resistance Updates : Reviews and Commentaries in Antimicrobial and Anticancer Chemotherapy
|November 10, 2006
PubMed

Insights

Aminoglycoside antibiotics fight bacterial infections by inhibiting protein synthesis. This review explores the diverse origins of aminoglycoside-modifying enzymes, a key mechanism of bacterial resistance.

Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Aminoglycosides are crucial antibiotics targeting bacterial protein synthesis.
  • In Gram-negative bacteria, they also disrupt the cell envelope.
  • Bacterial resistance often involves aminoglycoside-modifying enzymes (AMEs).

Purpose of the Study:

  • To review the diverse origins of aminoglycoside-modifying enzymes.
  • To discuss proposed evolutionary pathways for AMEs.
  • To explore mechanisms for the emergence of new AMEs.

Main Methods:

  • Literature review of existing studies on aminoglycoside resistance.
  • Analysis of proposed evolutionary origins of AMEs.
  • Discussion of potential mechanisms for AME development.

Main Results:

  • A wide array of AMEs exists in clinical bacterial isolates.
  • The diversity of AMEs suggests multiple evolutionary origins.
  • Previous proposals on AME origins are examined.

Conclusions:

  • The evolution of AMEs is complex, involving multiple origins.
  • Understanding AME evolution is critical for combating antibiotic resistance.
  • Further research into AME development mechanisms is warranted.

More Related Videos

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids11:56

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids

Published on: May 4, 2018

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü602809:08

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü6028

Published on: January 13, 2017

Related Concept Videos

Inhibitors of Bacterial Protein Synthesis01:25

Inhibitors of Bacterial Protein Synthesis

Aminoglycosides constitute a highly potent class of bactericidal antibiotics that exert their antimicrobial effects by targeting the bacterial ribosome, specifically disrupting protein synthesis. These polycationic molecules consist of amino-modified sugars linked via glycosidic bonds to an aminocyclitol core such as 2-deoxystreptamine or streptamine. Their strong positive charges facilitate tight binding to the negatively charged phosphate backbone of ribosomal RNA (rRNA), primarily at the 16S...
RNA Editing02:23

RNA Editing

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...
Transfer RNA Synthesis02:36

Transfer RNA Synthesis

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...
tRNA Activation02:26

tRNA Activation

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...
Amino Acid Catabolism01:18

Amino Acid Catabolism

Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
Pre-mRNA Processing: Modification of pre-mRNA Ends01:35

Pre-mRNA Processing: Modification of pre-mRNA Ends

In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
Once about 20-40 ribonucleotides have been joined together by RNA polymerase, a group of enzymes adds a cap to the 5' end of the growing transcript. In this process, a 5' phosphate is replaced by modified guanosine that has a methyl group attached (7-methyl guanosine). This 5' cap helps the cell...