AcmD, a homolog of the major autolysin AcmA of Lactococcus lactis, binds to the cell wall and contributes to cell separation and autolysis.
Lactococcus lactis expresses the homologous glucosaminidases AcmB, AcmC, AcmA and AcmD. The latter two have three C-terminal LysM repeats for peptidoglycan binding. AcmD has much shorter intervening sequences separating the LysM repeats and a lower iso-electric point (4.3) than AcmA (10.3). Under st...
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Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3738550?pdf=render |
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| author | Ganesh Ram R Visweswaran Anton Steen Kees Leenhouts Monika Szeliga Beata Ruban Anne Hesseling-Meinders Bauke W Dijkstra Oscar P Kuipers Jan Kok Girbe Buist |
| author_facet | Ganesh Ram R Visweswaran Anton Steen Kees Leenhouts Monika Szeliga Beata Ruban Anne Hesseling-Meinders Bauke W Dijkstra Oscar P Kuipers Jan Kok Girbe Buist |
| author_sort | Ganesh Ram R Visweswaran |
| collection | DOAJ |
| description | Lactococcus lactis expresses the homologous glucosaminidases AcmB, AcmC, AcmA and AcmD. The latter two have three C-terminal LysM repeats for peptidoglycan binding. AcmD has much shorter intervening sequences separating the LysM repeats and a lower iso-electric point (4.3) than AcmA (10.3). Under standard laboratory conditions AcmD was mainly secreted into the culture supernatant. An L. lactis acmAacmD double mutant formed longer chains than the acmA single mutant, indicating that AcmD contributes to cell separation. This phenotype could be complemented by plasmid-encoded expression of AcmD in the double mutant. No clear difference in cellular lysis and protein secretion was observed between both mutants. Nevertheless, overexpression of AcmD resulted in increased autolysis when AcmA was present (as in the wild type strain) or when AcmA was added to the culture medium of an AcmA-minus strain. Possibly, AcmD is mainly active within the cell wall, at places where proper conditions are present for its binding and catalytic activity. Various fusion proteins carrying either the three LysM repeats of AcmA or AcmD were used to study and compare their cell wall binding characteristics. Whereas binding of the LysM domain of AcmA took place at pHs ranging from 4 to 8, LysM domain of AcmD seems to bind strongest at pH 4. |
| first_indexed | 2024-12-24T03:14:16Z |
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| id | doaj.art-b4f2e91eb7c441ce81e320403dbf1b8e |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-24T03:14:16Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-b4f2e91eb7c441ce81e320403dbf1b8e2022-12-21T17:17:41ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0188e7216710.1371/journal.pone.0072167AcmD, a homolog of the major autolysin AcmA of Lactococcus lactis, binds to the cell wall and contributes to cell separation and autolysis.Ganesh Ram R VisweswaranAnton SteenKees LeenhoutsMonika SzeligaBeata RubanAnne Hesseling-MeindersBauke W DijkstraOscar P KuipersJan KokGirbe BuistLactococcus lactis expresses the homologous glucosaminidases AcmB, AcmC, AcmA and AcmD. The latter two have three C-terminal LysM repeats for peptidoglycan binding. AcmD has much shorter intervening sequences separating the LysM repeats and a lower iso-electric point (4.3) than AcmA (10.3). Under standard laboratory conditions AcmD was mainly secreted into the culture supernatant. An L. lactis acmAacmD double mutant formed longer chains than the acmA single mutant, indicating that AcmD contributes to cell separation. This phenotype could be complemented by plasmid-encoded expression of AcmD in the double mutant. No clear difference in cellular lysis and protein secretion was observed between both mutants. Nevertheless, overexpression of AcmD resulted in increased autolysis when AcmA was present (as in the wild type strain) or when AcmA was added to the culture medium of an AcmA-minus strain. Possibly, AcmD is mainly active within the cell wall, at places where proper conditions are present for its binding and catalytic activity. Various fusion proteins carrying either the three LysM repeats of AcmA or AcmD were used to study and compare their cell wall binding characteristics. Whereas binding of the LysM domain of AcmA took place at pHs ranging from 4 to 8, LysM domain of AcmD seems to bind strongest at pH 4.http://europepmc.org/articles/PMC3738550?pdf=render |
| spellingShingle | Ganesh Ram R Visweswaran Anton Steen Kees Leenhouts Monika Szeliga Beata Ruban Anne Hesseling-Meinders Bauke W Dijkstra Oscar P Kuipers Jan Kok Girbe Buist AcmD, a homolog of the major autolysin AcmA of Lactococcus lactis, binds to the cell wall and contributes to cell separation and autolysis. PLoS ONE |
| title | AcmD, a homolog of the major autolysin AcmA of Lactococcus lactis, binds to the cell wall and contributes to cell separation and autolysis. |
| title_full | AcmD, a homolog of the major autolysin AcmA of Lactococcus lactis, binds to the cell wall and contributes to cell separation and autolysis. |
| title_fullStr | AcmD, a homolog of the major autolysin AcmA of Lactococcus lactis, binds to the cell wall and contributes to cell separation and autolysis. |
| title_full_unstemmed | AcmD, a homolog of the major autolysin AcmA of Lactococcus lactis, binds to the cell wall and contributes to cell separation and autolysis. |
| title_short | AcmD, a homolog of the major autolysin AcmA of Lactococcus lactis, binds to the cell wall and contributes to cell separation and autolysis. |
| title_sort | acmd a homolog of the major autolysin acma of lactococcus lactis binds to the cell wall and contributes to cell separation and autolysis |
| url | http://europepmc.org/articles/PMC3738550?pdf=render |
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