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Structure, substrate recognition and initiation of hyaluronan synthase.

Finn P Maloney1, Jeremi Kuklewicz1, Robin A Corey2

  • 1Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA, USA.

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|March 31, 2022
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Researchers revealed the mechanism of hyaluronan synthase (HAS) in synthesizing hyaluronan, an essential extracellular matrix component. This study details how HAS selects substrates and forms the polymer, offering insights into glycosaminoglycan biosynthesis.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Extracellular Matrix Biology

Background:

  • Hyaluronan (HA) is a crucial extracellular matrix heteropolysaccharide involved in vital physiological processes.
  • Hyaluronan synthase (HAS) enzymes synthesize HA via a membrane-embedded process, utilizing activated sugar precursors.

Purpose of the Study:

  • To elucidate the molecular mechanism of hyaluronan synthesis by HAS.
  • To provide structural insights into substrate selection, polymerization, and product translocation during HA biosynthesis.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine structures of a viral HAS homologue.
  • Biochemical analyses to investigate enzyme activity.
  • Molecular dynamics simulations to model substrate interactions and polymerization.

Main Results:

  • Five cryo-EM structures captured HAS at various stages of substrate binding and polymer synthesis initiation.
  • The study reveals how HAS selects substrates, primes the reaction, forms a transmembrane channel, and ensures alternating polymerization.
  • A detailed model for hyaluronan formation and translocation through the HAS pore is proposed.

Conclusions:

  • The findings provide a comprehensive understanding of the biosynthesis of hyaluronan, a key glycosaminoglycan.
  • This research offers insights into the structure-function relationship of hyaluronan synthases.
  • The study illuminates the formation of acidic extracellular heteropolysaccharides.