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Modulation of domain-domain interaction and protein function by a charged linker: a case study of mycobacteriophage

Amol Arunrao Pohane1, Neelam Devidas Patidar1, Vikas Jain1

  • 1Microbiology and Molecular Biology Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research (IISER), Bhopal 462023, India.

FEBS Letters
|February 11, 2015
PubMed

Insights

Mycobacteriophage D29 endolysin inactivation in E. coli is due to intramolecular domain interaction. Charged linker composition is key for this peptidoglycan hydrolase inactivation, aiding endolysin bioengineering.

Area of Science:

  • Microbiology
  • Enzymology
  • Bioengineering

Background:

  • Bacteriophage endolysins are peptidoglycan hydrolases crucial for phage release.
  • Endolysins exhibit species-specific bacterial host killing.
  • Previous work showed mycobacteriophage D29 endolysin is inactive in E. coli due to domain interaction.

Purpose of the Study:

  • To elucidate the mechanism of mycobacteriophage D29 endolysin inactivation in E. coli.
  • To investigate the role of the linker connecting catalytic and binding domains.
  • To provide insights for bioengineering endolysins with tailored antimicrobial activity.

Main Methods:

  • Demonstration of intramolecular interaction between N-terminal catalytic and C-terminal cell wall binding domains.
  • Identification of a charged linker facilitating this intramolecular interaction.
  • Analysis of linker composition's effect on peptidoglycan hydrolase activity in E. coli.

Main Results:

  • The interaction between the catalytic and binding domains of D29 endolysin is intramolecular.
  • A charged linker region is essential for mediating this inactivating interaction.
  • Linker composition directly influences the enzyme's inactivation in E. coli.

Conclusions:

  • Understanding the intramolecular domain interaction and linker function is critical for endolysin activity.
  • This knowledge facilitates the rational design of endolysins for specific antimicrobial applications.
  • Bioengineering efforts can leverage linker composition to control endolysin spectrum and efficacy.
Keywords:
Activity regulationBacteriophageCell wall peptidoglycanCharged linkerDomain–domain interactionEndolysin

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