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It is well known that the Na +  cycle and the cell wall are essential for alkaline adaptation of Na + -dependent alkaliphilic  Bacillus  species. In  Bacillus pseudofirmus  OF4, surface layer protein A (SlpA), the most abundant protein in the surface layer (S-layer) of the cell wall, is involved in alkaline adaptation, especially under low Na +  concentrations. The presence of a large number of genes that encode S-layer homology (SLH) domain-containing proteins has been suggested from the genome sequence of  B. pseudofirmus  OF4. However, other than SlpA, the functions of SLH domain-containing proteins are not well known. Therefore, a deletion mutant of the  csaB  gene, required for the retention of SLH domain-containing proteins on the cell wall, was constructed to investigate its physiological properties. The  csaB  mutant strain of  B. pseudofirmus  OF4 had a chained morphology and alkaline sensitivity even under a 230 mM Na +  concentration at which there is no growth difference between the parental strain and the  slpA  mutant strain. Ultra-thin section transmission electron microscopy showed that a  csaB  mutant strain lacked an S-layer part, and its peptidoglycan (PG) layer was disturbed. The  slpA  mutant strain also lacked an S-layer part, although its PG layer was not disturbed. These results suggested that the surface layer homology domain-containing proteins of  B. pseudofirmus  OF4 play an important role in alkaline adaptation via peptidoglycan synthesis.

frontiers in microbiology

The Surface Layer Homology Domain-Containing Proteins of Alkaliphilic Bacillus pseudofirmus OF4 Play an Important Role in Alkaline Adaptation via Peptidoglycan Synthesis