ArticlePloS one2013
AcmD, a homolog of the major autolysin AcmA of Lactococcus lactis, binds to the cell wall and contributes to cell separation and autolysis.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Heterologous expression and purification of the phage lysin-like bacteriocin LysL from Lactococcus lactis LAC460.FEMS microbiology letters · 2024Article
- Extracellular vesicle formation in Lactococcus lactis is stimulated by prophage-encoded holin-lysin system.Microbial biotechnology · 2022Article
- Imbalance between peptidoglycan synthases and hydrolases regulated lysis of Lactobacillus bulgaricus in batch culture.Archives of microbiology · 2021Article
- Lysogenization of a Lactococcal Host with Three Distinct Temperate Phages Provides Homologous and Heterologous Phage Resistance.Microorganisms · 2020Article
- Another Breaker of the Wall: the Biological Function of the Usp45 Protein of Lactococcus lactis.Applied and environmental microbiology · 2020Article
- Domain sliding of two Staphylococcus aureus N-acetylglucosaminidases enables their substrate-binding prior to its catalysis.Communications biology · 2020Article
- Recovery of recombinant Mycobacterium tuberculosis antigens fused with cell wall-anchoring motif (LysM) from inclusion bodies using non-denaturing reagent (N-laurylsarcosine).BMC biotechnology · 2019Article
- Screening for New Surface Anchoring Domains forFrontiers in microbiology · 2019Article
- Article
- Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.Frontiers in microbiology · 2019Review
- Altering textural properties of fermented milk by using surface-engineered Lactococcus lactis.Microbial biotechnology · 2018Article
- Comparative Genomics ofFrontiers in microbiology · 2018Article
- Transcriptional Landscape of aFrontiers in microbiology · 2018Article
- A Lactococcus lactis expression vector set with multiple affinity tags to facilitate isolation and direct labeling of heterologous secreted proteins.Applied microbiology and biotechnology · 2017Article
- Diamide Inhibitors of the Bacillus subtilis N-Acetylglucosaminidase LytG That Exhibit Antibacterial Activity.ACS infectious diseases · 2017Article
- Expression of prophage-encoded endolysins contributes to autolysis of Lactococcus lactis.Applied microbiology and biotechnology · 2017Article
- Cell Surface Properties ofFrontiers in microbiology · 2017Article
- Identification and Functional Validation of Autolysis-Associated Genes inFrontiers in microbiology · 2017Article
- Identification of the chain-dispersing peptidoglycan hydrolase LytB of Streptococcus gordonii.PloS one · 2017Article
- Intracellular and Extracellular Expression of Bacillus thuringiensis Crystal Protein Cry5B in Lactococcus lactis for Use as an Anthelminthic.Applied and environmental microbiology · 2016Article
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Authors and funding
10 authors.
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No grant is acknowledged in the PubMed record.
Abstract
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.
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