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The SpoIIQ-SpoIIIAH complex of C lostridium difficile controls forespore engulfment and late stages of gene expression and spore morphogenesis.
- Source :
- Molecular Microbiology; Apr2016, Vol. 100 Issue 1, p204-228, 25p
- Publication Year :
- 2016
-
Abstract
- Engulfment of the forespore by the mother cell is a universal feature of endosporulation. In Bacillus subtilis, the forespore protein SpoIIQ and the mother cell protein SpoIIIAH form a channel, essential for endosporulation, through which the developing spore is nurtured. The two proteins also form a backup system for engulfment. Unlike in B. subtilis, SpoIIQ of Clostridium difficile has intact LytM zinc-binding motifs. We show that spoIIQ or spoIIIAH deletion mutants of C. difficile result in anomalous engulfment, and that disruption of the SpoIIQ LytM domain via a single amino acid substitution (H120S) impairs engulfment differently. SpoIIQ and SpoIIQ<superscript>H120S</superscript> interact with SpoIIIAH throughout engulfment. SpoIIQ, but not SpoIIQ<superscript>H120S</superscript>, binds Zn<superscript>2+</superscript>, and metal absence alters the SpoIIQ-SpoIIIAH complex in vitro. Possibly, SpoIIQ<superscript>H120S</superscript> supports normal engulfment in some cells but not a second function of the complex, required following engulfment completion. We show that cells of the spoIIQ or spoIIIAH mutants that complete engulfment are impaired in post-engulfment, forespore and mother cell-specific gene expression, suggesting a channel-like function. Both engulfment and a channel-like function may be ancestral functions of SpoIIQ-SpoIIIAH while the requirement for engulfment was alleviated through the emergence of redundant mechanisms in B. subtilis and related organisms. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 0950382X
- Volume :
- 100
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- Molecular Microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 113929061
- Full Text :
- https://doi.org/10.1111/mmi.13311