Bacillus brevis 47 cell walls feature a hexagonal protein array. A mutant lacking a key protein altered this array structure, impacting its unit cell composition.
Area of Science:
Microbiology
Structural Biology
Biochemistry
Background:
Bacillus brevis 47 is a protein-secreting bacterium.
Its cell wall possesses a distinct hexagonal array of structural units.
Purpose of the Study:
To investigate the structural organization of the Bacillus brevis 47 cell surface array.
To understand the role of major cell wall proteins in maintaining this array structure.
Main Methods:
Analysis of cell wall proteins using molecular weight determination.
Electron microscopy and image processing of wild-type and mutant cell envelopes.
Comparison of surface array structures between wild-type and mutant strains.
Main Results:
Wild-type Bacillus brevis 47 cell walls contain 150,000 and 130,000 molecular weight proteins, forming a hexagonal array with six units per cell.
A mutant strain (47-57) lacking the 130,000 protein showed altered array structure with three units per cell, despite maintaining the same lattice constant.
The array structure and composition were consistent across different growth conditions.
Conclusions:
The 130,000 molecular weight protein is crucial for the complete formation of the Bacillus brevis 47 surface array structure.
The study proposes two models for the surface array based on the observed differences between wild-type and mutant strains.