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Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
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Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
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The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is...
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Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
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Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
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Unlike mitosis, meiosis aims for genetic diversity in its creation of haploid gametes. Dividing germ cells first begin this process in prophase I, where each chromosome—replicated in S phase—is now composed of two sister chromatids (identical copies) joined centrally.
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Crossing over is the exchange of genetic information between homologous chromosomes during prophase I of meiosis I. Genetic recombination gives rise to allelic diversity in the newly formed daughter cells. In humans, crossing over produces genetically distinct haploid egg and sperm cells that undergo fertilization to produce unique offspring. Before cell division starts, the germ cell’s chromosome(s) undergo duplication in the S phase of the cell cycle. As the cells enter prophase I,...
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Lipid Exchange Assay in Living Cells
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Published on: March 21, 2025

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Crossing the lipid divide.

Christian Sohlenkamp1

  • 1Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Cuernavaca, Morelos, Mexico.

The Journal of Biological Chemistry
|June 7, 2021
PubMed
Summary

Researchers discovered a novel cardiolipin synthase enzyme in archaea. This enzyme synthesizes diverse cardiolipin lipids, paving the way for advancements in synthetic biology and novel lipid creation.

Area of Science:

  • Biochemistry
  • Synthetic Biology
  • Microbial Biochemistry

Background:

  • Archaeal membrane lipids exhibit unique structures compared to bacterial and eukaryotic lipids.
  • The enzymes responsible for archaeal lipid synthesis remain largely uncharacterized.
  • Cardiolipin is a key membrane lipid found across all domains of life.

Purpose of the Study:

  • To identify and characterize enzymes involved in archaeal membrane lipid synthesis.
  • To investigate the substrate specificity and product range of archaeal cardiolipin synthases.
  • To explore the potential of archaeal enzymes in synthetic lipid applications.

Main Methods:

  • Enzyme purification and characterization from Methanospirillum hungatei.
  • In vitro enzymatic assays to determine substrate and product profiles.
Keywords:
archaeal lipidsbacterial membranescardiolipincardiolipin synthasesynthetic biology

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  • Analysis of synthesized cardiolipin species using mass spectrometry.

    • Main Results:

    • A cardiolipin synthase was identified and characterized from Methanospirillum hungatei.
    • The enzyme demonstrated broad substrate specificity, synthesizing archaeal, bacterial, and mixed cardiolipin species.
    • The enzyme could utilize non-natural substrates, producing lipids with novel head groups and hydrophobic chains.

    Conclusions:

    • The identified cardiolipin synthase possesses versatile synthetic capabilities.
    • This enzyme offers a powerful tool for constructing diverse and non-natural cardiolipin lipids.
    • The findings have significant implications for the field of synthetic lipid biology.