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Updated: Jun 3, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

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Published on: December 17, 2013

Structure-function analysis of the bacterial expansin EXLX1.

Nikolaos Georgelis1, Akira Tabuchi, Nikolas Nikolaidis

  • 1Department of Biology, Pennsylvania State University, University Park, Pennsylvania 16802, USA.

The Journal of Biological Chemistry
|April 2, 2011
PubMed
Summary

This study reveals key features of bacterial expansin EXLX1 for plant cell wall interaction. Specific residues in its D2 domain are crucial for cellulose binding and wall loosening, offering insights into plant expansin function.

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Last Updated: Jun 3, 2026

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Published on: July 4, 2016

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Plant Science

Background:

  • Expansins are proteins that facilitate plant cell wall loosening, essential for growth.
  • Understanding the molecular mechanisms of expansin-cell wall interactions is crucial for agricultural applications.

Purpose of the Study:

  • To investigate the specific protein features of Bacillus subtilis expansin EXLX1 responsible for its plant cell wall binding and loosening activities.
  • To elucidate the roles of its two domains (D1 and D2) and specific amino acid residues in these functions.

Main Methods:

  • Site-directed mutagenesis of EXLX1 to alter specific amino acid residues.
  • Assays to measure protein binding to isolated cell walls and cellulose.
  • Measurement of wall loosening activity using cell wall extension and filter paper weakening assays.

Main Results:

  • The two expansin domains, D1 and D2, must be linked for wall extension activity.
  • Distinct residues on domain D2 mediate binding to whole cell walls (basic residues) and cellulose (aromatic residues).
  • Mutation of cellulose-binding aromatic residues abolished cellulose binding and wall loosening, while mutation of basic residues reduced cell wall binding but not wall loosening.

Conclusions:

  • Domain D2 is proposed as a founding member of a new carbohydrate-binding module family (CBM63), with functions beyond simple anchoring.
  • Specific polar residues in domain D1, like Asp82, are critical for wall loosening activity.
  • Functional insights from bacterial EXLX1 can inform the study of plant expansin-cell wall interactions.