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Related Concept Videos

Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

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Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
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Protein Diffusion in the Membrane01:24

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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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Insertion of Multi-pass Transmembrane Proteins in the RER01:29

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The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
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IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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Related Experiment Video

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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Single transmembrane peptide DinQ modulates membrane-dependent activities.

Ragnhild Weel-Sneve1, Knut Ivan Kristiansen, Ingvild Odsbu

  • 1Centre for Molecular Biology and Neuroscience (CMBN), University of Oslo and Oslo University Hospital, Rikshospitalet, Oslo, Norway.

Plos Genetics
|February 15, 2013
PubMed
Summary

This study characterizes the dinQ gene in Escherichia coli, revealing its toxic peptide product regulated by AgrB RNA interference. This dinQ-agr locus functions as a type I toxin-antitoxin system impacting membrane processes and recombination.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Genetics

Background:

  • The SOS response in Escherichia coli regulates numerous genes, but the functions of some, like dinQ, remain unclear.
  • Small regulatory RNAs play crucial roles in gene expression, particularly in stress responses.

Purpose of the Study:

  • To characterize the function of the dinQ gene and its regulatory small RNAs, agrA and agrB, in Escherichia coli.
  • To elucidate the role of dinQ in cellular processes, including membrane function, recombination, and response to DNA damage.

Main Methods:

  • Northern blot analysis to identify dinQ transcripts.
  • RNA interference assays to study AgrB regulation of dinQ.
  • Assessment of membrane potential and intracellular ATP levels upon dinQ overexpression.
  • Hfr conjugation experiments to evaluate recombination inhibition.
  • Microscopy to observe nucleoid morphology changes.

Main Results:

  • Five dinQ transcripts were identified, with only one (+44) being actively translated into a toxic inner membrane peptide.
  • AgrB acts as an RNA interference regulator, counteracting DinQ toxicity, establishing the dinQ-agr locus as a type I toxin-antitoxin system.
  • DinQ overexpression disrupts cell membrane potential, reduces intracellular ATP, inhibits Hfr conjugation-mediated marker transfer, and alters nucleoid morphology post-UV damage.

Conclusions:

  • DinQ is a toxic transmembrane peptide involved in modulating membrane-dependent processes and recombination in Escherichia coli.
  • The dinQ-agr locus represents a novel type I toxin-antitoxin system with functional similarities to the tisB-istR locus.
  • DinQ likely plays a role in nucleoid compaction and recombination, particularly under stress conditions like UV damage.