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Cross-linking of contractile proteins from skeletal muscle by treatment with microbial transglutaminase

Y P Huang1, K Seguro, M Motoki

  • 1Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka.

Journal of Biochemistry
|August 1, 1992
PubMed

Insights

Microbial transglutaminase (MTGase) cross-links myosin filaments but not actin. This enzyme minimally impacts myosin

Area of Science:

  • Muscle protein biochemistry
  • Enzymology
  • Biotechnology

Background:

  • Microbial transglutaminase (MTGase) forms covalent cross-links between glutamine and lysine residues.
  • Understanding MTGase's action on muscle proteins is crucial for protein interaction studies.
  • MTGase offers potential for investigating muscle protein dynamics.

Purpose of the Study:

  • To investigate microbial transglutaminase (MTGase) cross-linking of skeletal muscle proteins.
  • To assess the impact of MTGase on myosin and actin interactions.
  • To evaluate potential side-effects on myosin enzymatic activity.

Main Methods:

  • Treatment of myosin, myosin subfragments, actin, and myofibrils with MTGase.
  • Analysis of cross-linking patterns using biochemical assays.
  • Measurement of MgATPase activities to assess enzymatic function.

Main Results:

  • MTGase rapidly cross-linked the rod portions of myosin within filaments.
  • Myosin subfragment 1 did not show cross-linking with actin.
  • MgATPase activities of various myosin preparations were largely unaffected by MTGase.
  • A minor cross-link formed between heavy meromyosin heads and actin in rigor complexes, slightly enhancing ATPase activity.

Conclusions:

  • MTGase effectively cross-links myosin filaments, providing a tool for structural studies.
  • MTGase exhibits minimal detrimental effects on myosin enzymatic activity.
  • Specific cross-linking of myosin heads to actin occurs in rigor complexes, with a slight ATPase enhancement.

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