Journal
MICROORGANISMS
Volume 9, Issue 2, Pages -Publisher
MDPI
DOI: 10.3390/microorganisms9020409
Keywords
Corynebacterium glutamicum; LtsA; cell-surface structure; mycolic acid
Categories
Funding
- Japan Society for the Promotion of Science [15380059]
- Grants-in-Aid for Scientific Research [15380059] Funding Source: KAKEN
Ask authors/readers for more resources
The study investigated the intracellular localization of wild-type and mutant LtsA proteins fused with GFP, revealing that the C-terminal domain is required for peripheral localization. Furthermore, differential staining of cell wall structures showed that the ltsA mutant cells had impaired formation of the mycolic acid-containing layer at the cell division planes, leading to increased susceptibility to lysozyme.
The ltsA gene of Corynebacterium glutamicum encodes a purF-type glutamine-dependent amidotransferase, and mutations in this gene result in increased susceptibility to lysozyme. Recently, it was shown that the LtsA protein catalyzes the amidation of diaminopimelate residues in the lipid intermediates of peptidoglycan biosynthesis. In this study, intracellular localization of wild-type and mutant LtsA proteins fused with green fluorescent protein (GFP) was investigated. The GFP-fused wild-type LtsA protein showed a peripheral localization pattern characteristic of membrane-associated proteins. The GFP-fusions with a mutation in the N-terminal domain of LtsA, which is necessary for the glutamine amido transfer reaction, exhibited a similar localization to the wild type, whereas those with a mutation or a truncation in the C-terminal domain, which is not conserved among the purF-type glutamine-dependent amidotransferases, did not. These results suggest that the C-terminal domain is required for peripheral localization. Differential staining of cell wall structures with fluorescent dyes revealed that formation of the mycolic acid-containing layer at the cell division planes was affected in the ltsA mutant cells. This was also confirmed by observation that bulge formation was induced at the cell division planes in the ltsA mutant cells upon lysozyme treatment. These results suggest that the LtsA protein function is required for the formation of a mycolic acid-containing layer at the cell division planes and that this impairment results in increased susceptibility to lysozyme.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available