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Updated: Jul 15, 2026

The Multifaceted Benefits of Protein Co-expression in Escherichia coli
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Published on: February 5, 2015

ElaD, a Deubiquitinating protease expressed by E. coli.

André Catic1, Shahram Misaghi, Gregory A Korbel

  • 1Immunology Program, Harvard Medical School, Boston, Massachusetts, United States of America.

Plos One
|April 19, 2007
PubMed
Summary

Researchers identified the E. coli protein ElaD as a deubiquitinating enzyme, crucial for reversing protein modifications. This enzyme is found in intestinal pathogens but not extraintestinal ones, suggesting a role in pathogenesis.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Ubiquitin and ubiquitin-like proteins (Ubl) are key post-translational modifiers in eukaryotes.
  • Specific hydrolases, including the CE clan of cysteine proteases, reverse these modifications.
  • Homologs of these proteases exist across eukaryotes, prokaryotes, and viruses.

Purpose of the Study:

  • To characterize the E. coli protein ElaD, previously misannotated.
  • To investigate the function and distribution of ElaD and its homologs.
  • To explore the evolutionary origins of ubiquitin-specific hydrolases.

Main Methods:

  • Cloning and in vitro analysis of the E. coli protein ElaD.
  • Phylogenetic examination of protease homologs.
  • Functional analysis of ElaD and related bacterial hydrolases.

Main Results:

  • ElaD functions as an efficient and specific deubiquitinating enzyme.
  • ElaD is present in intestinal pathogenic E. coli but absent in extraintestinal pathogenic strains.
  • Homologs of ElaD are found in various bacteria, viruses, and eukaryotes.

Conclusions:

  • The study reveals ElaD as a bacterial deubiquitinating enzyme with potential roles in pathogenesis.
  • Orthologs like SseL in other bacteria are confirmed virulence factors with deubiquitinating activity.
  • Eukaryotic ULP/SENP proteases share ancient origins with bacterial counterparts, highlighting conserved hydrolysis mechanisms.