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Related Concept Videos

Prokaryotic Transcriptional Activators and Repressors01:58

Prokaryotic Transcriptional Activators and Repressors

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The organization of prokaryotic genes in their genome is notably different from that of eukaryotes. Prokaryotic genes are organized, such that the genes for proteins involved in the same biochemical process or function are located together in groups. This group of genes, along with their regulatory elements, are collectively known as an operon. The functional genes in an operon are transcribed together to give a single strand of mRNA known as polycistronic mRNA.
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Replication in Prokaryotes01:32

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DNA replication has three main steps: initiation, elongation, and termination. Replication in prokaryotes begins when initiator proteins bind to the single origin of replication (ori) on the cell's circular chromosome. Replication then proceeds around the entire circle of the chromosome in each direction from the two replication forks, resulting in two DNA molecules.
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Comparing Mitochondrial, Chloroplast, and Prokaryotic Genomes02:16

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The present-day mitochondrial and chloroplast genomes have retained some of the characteristics of their ancestral prokaryotes and also have acquired new attributes during their evolution within eukaryotic cells. Like prokaryotic genomes, mitochondrial and chloroplast genomes neither bind with histone-like proteins nor show complex packaging into chromosome-like structures, as observed in eukaryotes. Unlike mitotic cell divisions observed in eukaryotic cells, mitochondria and chloroplasts...
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Histone Modification02:32

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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Transcription Attenuation in Prokaryotes02:42

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Transcriptional attenuation occurs when RNA transcription is prematurely terminated due to the formation of a terminator mRNA hairpin structure.  Bacteria use these hairpins to regulate the transcription process and control the synthesis of several amino acids including histidine, lysine, threonine, and phenylalanine. Transcription attenuation takes place in the non-coding regions of mRNA.
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Related Experiment Video

Updated: Feb 4, 2026

Purification of Tubulin with Controlled Posttranslational Modifications and Isotypes from Limited Sources by Polymerization-Depolymerization Cycles
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Characterizing posttranslational modifications in prokaryotic metabolism using a multiscale workflow.

Elizabeth Brunk1,2, Roger L Chang3,4, Jing Xia5

  • 1Department of Bioengineering, University of California, San Diego, La Jolla, CA 92093.

Proceedings of the National Academy of Sciences of the United States of America
|October 11, 2018
PubMed
Summary
This summary is machine-generated.

This study introduces a new workflow combining genome editing, metabolic modeling, and molecular dynamics to understand how protein posttranslational modifications (PTMs) affect microbial fitness and enzyme function. The findings reveal PTMs

Keywords:
metabolismomics dataposttranslational modificationsprotein chemistrysystems biology

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Area of Science:

  • Biochemistry
  • Systems Biology
  • Molecular Biology

Background:

  • Protein posttranslational modifications (PTMs) are crucial for cellular functions but challenging to study.
  • Understanding PTMs' impact on metabolic enzymes and microbial fitness is vital for metabolic engineering and synthetic biology.

Purpose of the Study:

  • To develop and validate an integrated workflow for studying PTM effects on metabolic enzymes and microbial fitness.
  • To provide molecular insights into how PTMs influence cellular behavior during nutrient fluctuations.

Main Methods:

  • Integration of multiplex automated genome editing (MAGE), genome-scale metabolic modeling, and atomistic molecular dynamics.
  • Global analysis of PTMs in the *Escherichia coli* metabolic network.
  • Detailed mechanistic analysis of PTMs in key metabolic enzymes (enolase, serine hydroxymethyltransferase, transaldolase).

Main Results:

  • The workflow successfully linked specific PTMs to observed experimental phenomena.
  • Identified how individual PTMs regulate enzyme activity, metabolic pathways, and overall cell phenotypes.
  • Demonstrated the ability to explore PTM mechanisms across different biological scales.

Conclusions:

  • The presented workflow offers a powerful, multidisciplinary approach to dissecting the functional roles of PTMs.
  • Mechanistic understanding of PTMs can be achieved through integrating computational and experimental techniques.
  • This approach advances the study of PTMs in metabolic engineering, synthetic biology, and biomedical research.