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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

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Spanin function requires subunit homodimerization through intermolecular disulfide bonds.

Joel D Berry¹, Manoj Rajaure, Ry Young

¹Center for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, USA.

Molecular Microbiology

|February 8, 2013

Summary

This summary is machine-generated.

The spanin proteins Rz and Rz1 form homodimers via disulfide bonds, crucial for outer membrane disruption during host lysis. Spanin function depends on specific disulfide linkages, with DsbA involvement in Rz homodimer formation.

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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Area of Science:

Bacteriology
Molecular Biology
Protein Chemistry

Background:

The spanin complex, comprising Rz (i-spanin) and Rz1 (o-spanin), is essential for bacterial outer membrane disruption during host cell lysis.
Rz features an alpha-helical periplasmic domain, while Rz1 has a proline-rich structure lacking predicted secondary elements.

Purpose of the Study:

To investigate the covalent structure of Rz and Rz1 homodimers.
To determine the role of specific intermolecular disulfide bonds in spanin complex function.
To elucidate the involvement of host disulfide bond formation pathways (DsbA, DsbC) in spanin assembly and function.

Main Methods:

Analysis of Rz and Rz1 homodimer formation via intermolecular disulfide bonds.
Mutational analysis of cysteine residues involved in disulfide bond formation.
Assessment of spanin function in wild-type and dsb mutant bacterial hosts (dsbA, dsbC, dsbA dsbC).

Main Results:

Both Rz and Rz1 form homodimers covalently linked by intermolecular disulfide bonds involving all three cysteine residues.
Spanin function requires at least one of two specific disulfide linkages: the Rz1-Rz1 bond or the distal Rz-Rz bond.
Rz homodimer formation is impaired in dsbC hosts, suggesting DsbA-mediated intramolecular disulfide formation in Rz is part of the normal pathway.
Efficient Rz1-Rz1 disulfide bond formation requires DsbA.
Dsb-independent homodimer formation necessitates the presence of the other subunit, likely acting as a template.

Conclusions:

Specific intermolecular disulfide bonds in Rz and Rz1 homodimers are critical for spanin-mediated outer membrane disruption.
The bacterial disulfide bond pathway, particularly DsbA, plays a significant role in the proper assembly and function of the spanin complex.
The formation of covalent spanin homodimers is a key step in the lysis process, influenced by both intrinsic protein properties and host cellular machinery.