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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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Elastin is heterogeneously cross-linked.

Christoph U Schräder1, Andrea Heinz1,2, Petra Majovsky3

  • 1From the Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale) 06120, Germany.

The Journal of Biological Chemistry
|August 16, 2018
PubMed
Summary
This summary is machine-generated.

Elastin cross-linking involves random connections between tropoelastin monomers, forming an unordered network. This study reveals diverse cross-link types and unexpected intramolecular bonds in mature elastin.

Keywords:
allysine aldoldesmosineelastic fiberselastinextracellular matrix proteinlysinonorleucinelysyl oxidasemass spectrometry (MS)protein cross-linkingprotein structure

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Materials Science

Background:

  • Elastin is a vital vertebrate protein providing elasticity to tissues like lungs, blood vessels, and skin.
  • Extensive covalent cross-linking of tropoelastin monomers is crucial for elastin's unique mechanical properties.
  • The precise molecular assembly and mechanical characteristics of elastin remain incompletely understood.

Purpose of the Study:

  • To investigate the diverse cross-link types present in mature elastin.
  • To elucidate the molecular structure and assembly of elastin.
  • To gain insights into the relationship between elastin structure and its mechanical properties.

Main Methods:

  • Purification and proteolytic cleavage of bovine elastin.
  • Analysis of soluble cross-linked and non-cross-linked peptides using high-resolution mass spectrometry (MS).
  • Elucidation of cross-links and other modifications in tropoelastin.

Main Results:

  • Lysine residues in tropoelastin are involved in various cross-links and can also be unmodified.
  • Lys-Pro domains are primarily linked by lysinonorleucine.
  • Lys-Ala domains exhibit cross-linking via lysinonorleucine, allysine aldol, and desmosine, with a significant number of intramolecular cross-links observed.

Conclusions:

  • Elastin formation involves random cross-linking of tropoelastin monomers, creating an unordered network.
  • This finding contrasts with previous assumptions of a more ordered, beaded elastin structure.
  • The study provides molecular-level insights into elastin's complex cross-linking and network formation.