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Related Concept Videos

Translational Regulation01:29

Translational Regulation

Translational regulation in prokaryotes ensures efficient protein synthesis by controlling ribosome access to mRNA. This regulation is mediated by secondary RNA structures, including translational riboswitches, RNA thermometers, and small RNAs (sRNAs), which respond to intracellular and environmental signals to modulate gene expression.Translational RiboswitchesRiboswitches in the leader region of mRNAs can regulate translation by altering the accessibility of the Shine-Dalgarno (SD) sequence,...
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MicroRNAs

MicroRNA (miRNA) are short, regulatory RNA transcribed from introns—non-coding regions of a gene—or intergenic regions—stretches of DNA present between genes. Several processing steps are required to form biologically active, mature miRNA. The initial transcript, called primary miRNA (pri-mRNA), base-pairs with itself forming a stem-loop structure. Within the nucleus, an endonuclease enzyme, called Drosha, shortens the stem-loop structure into hairpin-shaped pre-miRNA. After the pre-miRNA ends...
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Inhibitors of Bacterial Protein Synthesis01:25

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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...
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Types of RNA

Overview
Three main types of RNA are involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). These RNAs perform diverse functions and can be broadly classified as protein-coding or non-coding RNA. Non-coding RNAs play important roles in the regulation of gene expression in response to developmental and environmental changes. Non-coding RNAs in prokaryotes can be manipulated to develop more effective antibacterial drugs for human or animal use.
RNA...
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Leaky Scanning

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 stands for...

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Low-molecular-weight post-translationally modified microcins.

Konstantin Severinov1, Ekaterina Semenova, Alexey Kazakov

  • 1Waksman Institute for Microbiology, Rutgers, the State University of New Jersey, Piscataway, NJ 08854, USA. severik@waksman.rutgers.edu

Molecular Microbiology
|August 23, 2007
PubMed
Summary

This review details three post-translationally modified microcins (microcin J25, B17, and C7-C51) from Escherichia coli. These low-molecular-weight antibacterial peptides target essential cellular machinery, offering insights into bacterial defense mechanisms.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Microcins are ribosomally synthesized antibacterial peptides produced by Enterobacteriaceae.
  • Some microcins undergo post-translational modification by dedicated enzymes, affecting their activity.
  • Low-molecular-weight, modified microcins target essential intracellular molecular machines.

Purpose of the Study:

  • To review available structural and functional data on three specific microcins: microcin J25, microcin B17, and microcin C7-C51.
  • To discuss the characteristics of these low-molecular-weight, post-translationally modified microcins.
  • To place these microcins within a broader context by comparing them to similar peptides from diverse bacterial species.

Main Methods:

  • Literature review of structural and functional data.
  • Comparative analysis of sequence and structural similarities.
  • Inferences based on phylogenetic diversity of producing bacteria.

Main Results:

  • Detailed discussion of microcin J25, microcin B17, and microcin C7-C51 structures and functions.
  • Identification of these three microcins as low-molecular-weight, post-translationally modified antibacterial peptides.
  • Exploration of potential broader roles and origins of these microcin classes.

Conclusions:

  • Post-translationally modified microcins represent a significant class of antibacterial agents with diverse structures and targets.
  • Comparative analysis aids in understanding the evolution and distribution of microcin systems.
  • Further research into these microcins can inform the development of novel antimicrobial strategies.