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Structural basis for human chondroitin sulfate chain polymerization.

Poushalee Dutta1, Rosa L Cordeiro1, Mélanie Friedel-Arboleas1

  • 1Institut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, CEA, Grenoble, France.

Nature Communications
|November 26, 2025
PubMed
Summary
This summary is machine-generated.

Researchers identified four human enzyme complexes, including chondroitin sulfate synthase 1 (CHSY1) and CHSY3, that build chondroitin sulfate chains. These findings reveal the polymerization mechanism and catalytic roles within these crucial biological molecules.

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Structural Biology

Background:

  • Chondroitin sulfates are vital polysaccharides involved in cell surface and extracellular matrix functions.
  • Understanding chondroitin sulfate biosynthesis is crucial for deciphering its regulatory roles in biological processes.

Purpose of the Study:

  • To identify and characterize the human enzyme complexes responsible for chondroitin sulfate chain polymerization.
  • To elucidate the molecular mechanism and catalytic activities involved in chondroitin sulfate synthesis.

Main Methods:

  • Development of a chemo-enzymatic in vitro glycosylation assay using fluorescent substrates.
  • Cryo-electron microscopy (cryo-EM) to determine the structure of the CHSY3-CHPF complex.
  • Mutational analysis and in cellulo complementation assays to validate enzyme function.

Main Results:

  • Four heterodimeric complexes (CHSY1-CHPF, CHSY1-CHPF2, CHSY3-CHPF, CHSY3-CHPF2) were identified as responsible for chondroitin sulfate polymerization.
  • All identified complexes demonstrated chain polymerization activity in vitro.
  • Structural and mutational analyses revealed CHSY1 and CHSY3 as the enzymatically active components, with CHPF and CHPF2 playing stabilizing roles.
  • The study proposes a non-processive, distributive mechanism for chondroitin sulfate chain polymerization based on catalytic site arrangement.

Conclusions:

  • The identified enzyme complexes and their distinct roles provide a molecular basis for chondroitin sulfate biosynthesis.
  • CHSY1 and CHSY3 possess bifunctional glycosyltransferase activities essential for polymerization.
  • The proposed polymerization mechanism offers new insights into the regulation of chondroitin sulfate structure and function.