AI Article Synopsis
- The expression of the iap gene in Listeria monocytogenes rough mutant RIII and Bacillus subtilis DB104 disrupts their usual cell chain formation during exponential growth.
- The p60 protein from both organisms shows bacteriolytic activity, which was confirmed through specific testing methods.
- A conserved cysteine in the p60 protein is crucial for its function, and since the iap gene can't be inactivated without killing the cells, p60 is essential for cell viability in Listeria species, suggesting it plays a key role in cell division.
Article Abstract
Expression of the iap gene of Listeria monocytogenes in the L. monocytogenes rough mutant RIII and in Bacillus subtilis DB104 caused the disruption of the cell chains which these two strains normally form under exponential growth conditions. The p60 protein produced by L. monocytogenes and B. subtilis DB104 also exhibited bacteriolytic activity detected in denaturing polyacrylamide gels containing heat-killed Micrococcus lysodeikticus. Purification of the p60 protein led to aggregation of p60 and loss of the cell chain disruption and bacteriolytic activities. A cysteine residue in the C-terminal part of p60 which is conserved in all p60-like proteins from the other Listeria species seems to be essential for both activities. The iap gene could not be inactivated without a loss of cell viability, indicating that p60 is an essential housekeeping protein for L. monocytogenes and probably also for other Listeria species. These data suggest that p60 possesses a murein hydrolase activity required for a late step in cell division.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC204749 | PMC |
| http://dx.doi.org/10.1128/jb.175.11.3491-3501.1993 | DOI Listing |
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