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A Deep-sequencing-assisted, Spontaneous Suppressor Screen in the Fission Yeast Schizosaccharomyces pombe

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Suppressor Analysis of the Fusogenic Lambda Spanins.

Jesse Cahill¹, Manoj Rajaure¹, Ashley Holt¹

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

Journal of Virology

|May 5, 2017

Summary

This summary is machine-generated.

Bacteriophage lambda spanins Rz and Rz1 mediate cell lysis by fusing bacterial membranes. Suppressor mutations destabilize a key protein complex, restoring function by increasing flexibility, albeit with altered lysis timing.

Keywords:

Escherichia coli bacteriophage lysis coiled coil membrane fusion phage

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Area of Science:

Microbiology
Molecular Biology
Virology

Background:

Bacteriophage lambda lysis of Escherichia coli involves spanins Rz and Rz1.
Spanins are proposed to fuse the bacterial inner and outer membranes, essential for phage release.
Understanding spanin function is crucial for deciphering viral lysis mechanisms.

Purpose of the Study:

To investigate the function of lambda spanins Rz and Rz1 through suppressor analysis.
To identify key domains and conformational changes involved in spanin-mediated membrane fusion.
To gain insights into the intermediate structures of viral fusion systems.

Main Methods:

Selection of pseudorevertant alleles restoring lysis in defective spanin mutants.
Analysis of second-site suppressor mutations within the Rz coiled-coil domain.
Assessment of proteolytic stability and cell morphology changes in Rz mutants.

Main Results:

Suppressor mutations clustered in a coiled-coil domain of Rz, causing polar insertions.
These mutations decreased proteolytic stability of spanin complexes.
Mutant cells formed spherical shapes before lysis, unlike wild-type rod-shaped cells.

Conclusions:

Destabilizing the membrane-proximal coiled coil restores function to defective spanin alleles.
Increased conformational freedom of the spanin complex may underlie restored function.
This study provides the first suppressor analysis of a class I-like fusion complex in prokaryotes.