Cloning and nucleotide sequence of the gene encoding the γ-?-glutamyl-?-diamino acid endopeptidase II of Bacillus sphaericus

Hourdou, Marie-Laure

doi:10.1016/0378-1097(92)90678-h

Cited by 11 publications

(15 citation statements)

References 7 publications

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“…Four of them, the previously characterized AcmA and AcmB proteins as well as the putative enzymes AcmC and AcmD, belong to the family of enterococcal muramidases (12). Conversely, YjgB has similarity with the active-site domain of peptidoglycan-specific endopeptidases (23). All of them possess a putative signal peptide sequence at the N terminus (31).…”

Section: Resultsmentioning

confidence: 99%

Analysis of the Peptidoglycan Hydrolase Complement of Lactococcus lactis : Identification of a Third N- Acetylglucosaminidase, AcmC

Huard

Miranda

Redko

et al. 2004

Appl Environ Microbiol

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The peptidoglycan hydrolase (PGH) complement of Lactococcus lactis was identified by amino acid sequence similarity searching of the L. lactis IL-1403 complete genome sequence. Five PGHs that are not encoded by prophages were detected, including the previously characterized AcmA and AcmB proteins. Four of these PGHs, AcmA to AcmD, contain a catalytic domain homologous to that of enterococcal muramidase, but they have different domain structures. The fifth one (YjgB) has sequence similarity with the active-site domain of peptidoglycan-specific endopeptidases. The three new PGH-encoding genes identified in this study are all actively transcribed in L. lactis subsp. cremoris MG1363. The relative abundance of their transcripts varied during growth and was maximal during the early exponential growth phase. The three encoded proteins have peptidoglycan-hydrolyzing activities which are detected only at acidic pHs by zymography. Like AcmA and AcmB, AcmC has N-acetylglucosaminidase activity rather than the N-acetylmuramidase activity predicted by sequence similarity.

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Section: Resultsmentioning

confidence: 99%

Analysis of the Peptidoglycan Hydrolase Complement of Lactococcus lactis : Identification of a Third N- Acetylglucosaminidase, AcmC

Huard

Miranda

Redko

et al. 2004

Appl Environ Microbiol

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“…More interestingly, the N-terminal sequence of the 0.001 M NaCl-eluting protein was found to be similar to a number of proteins belonging to the P60 superfamily. This family essentially comprises a range of bacterial proteins with diverse biological properties and include Listerial P60 proteins [38,39], invasion-associated proteins from Mycobacteria [40^42], a protein of unknown function from Streptomyces coelicolor [43], putative amylase from Clostridial species [44,45], D-glutamyl-L-diamino acid endopeptidase from Bacillus sphaericus [46,47], Enterococcus faecium P54 precursor protein [48] and the LytF hydrolase from Bacillus subtilis [49,50].…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterisation of a 13.8-kDa bacteriolytic enzyme from house dust mite extracts: homology with prokaryotic proteins suggests that the enzyme could be bacterially derived

Mathaba¹

2002

FEMS Immunology and Medical Microbiology

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Bacteriolytic activity was detected in extracts of whole mite and spent growth medium (SGM) from the clinically important Dermatophagoides pteronyssinus and Dermatophagoides farinae mites and was most abundant in whole mite extract. Gram-positive organisms Micrococcus lysodeikticus, Bacillus megaterium and Listeria monocytogenes were preferentially lysed and the lytic activity was enhanced by thiols, destroyed by mite proteases, inhibited by HgCl2 and high concentrations of NaCl but was resistant to heat and acid treatment. Substrate SDS-PAGE analysis indicated the presence of several lytic enzymes, two of which were isolated from D. pteronyssinus spent growth medium extract by hydroxyapatite chromatography. The N-terminal amino acid sequence of one of them was then used in PCR-based cloning studies. The complete amino acid sequence of this protein was determined and cDNA found to encode a 130-amino acid residue mature protein with a 20-amino acid leader sequence. The deduced protein demonstrated sequence similarity with the C-terminal regions of a group of bacterial proteins belonging to the P60 superfamily. These data suggest that the enzyme is derived from bacteria within the mites rather than from mites per se.

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“…Its peptidoglycan-hydrolyzing activity was confirmed in zymogram assays (16). The fifth PGH of L. lactis, YjgB, shows sequence similarity with the active site domain of peptidoglycan-specific endopeptidases, such as LytE and LytF from B. subtilis (18,23,24) or the ␥-D-Glu-(L)-mesodiaminopimelic acid-endopeptidase from Bacillus sphaericus (15). Its peptidoglycan-hydrolyzing activity was previously detected by zymogram assay under native conditions, in a gel without sodium dodecyl sulfate (SDS), but its hydrolytic specificity was not determined (16).…”

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confidence: 96%

Lactococcus lactis Gene yjgB Encodes a γ- d -Glutaminyl- l -Lysyl- Endopeptidase Which Hydrolyzes Peptidoglycan

Redko

Courtin

Mézange

et al. 2007

Appl Environ Microbiol

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YjgB is one of five peptidoglycan hydrolases previously identified in Lactococcus lactis. Analysis of its amino acid sequence revealed that YjgB contains an NlpC/P60 domain, whereas no specific cell wall binding domain or motif could be identified. The NlpC/P60 family is characterized by three conserved residues, a cysteine, a histidine, and a polar residue. In agreement with the presence of a Cys residue in the catalytic site of YjgB, its enzymatic activity was enhanced in the presence of dithiothreitol. Peptidoglycan-hydrolyzing activity of YjgB was detected in growing cells of an L. lactis strain overexpressing YjgB, as revealed by the presence of disaccharide (DS)-dipeptide in the muropeptide composition of the overexpressing strain. YjgB hydrolyzes the peptide chains of L. lactis muropeptides between ␥-D-Gln and L-Lys residues. Its hydrolytic activity was detected on DSs with tetra-and pentapeptide chains, whereas hydrolytic activity was very low on DS-tripeptides. Thus, we demonstrated that YjgB is an endopeptidase which cleaves ␥-D-Gln-L-Lys bonds in peptide chains of L. lactis peptidoglycan.The cell integrity of gram-positive bacteria is ensured by a cell wall which consists mainly of peptidoglycan, an aminosugar polymer cross-linked with peptide bridges. Peptidoglycan metabolism is a necessary process in cell wall remodeling during growth and cell division, during which peptidoglycan hydrolysis is balanced with the synthesis of new polymer blocks (9, 31). While cell integrity is in this case maintained, it is compromised during cellular autolysis. Both processes require the action of enzymes called peptidoglycan hydrolases (PGHs), which catalyze cleavage of peptidoglycan sugar or peptide chains. In lactic acid bacteria such as Lactococcus lactis, which is used as a dairy starter, PGH activity during cheese ripening leads to cellular autolysis and release of the cellular content to the cheese curd. This provides the pool of enzymes acting in the development of organoleptic properties of cheese (22). Therefore, control of PGH activity in L. lactis bears the potential for control of cheese ripening in industrial conditions. The PGH complement of L. lactis was analyzed previously and comprises five PGHs (16). It includes AcmA, AcmB, and AcmC, all of which exhibit N-acetylglucosaminidase hydrolytic specificity (16,17,32). AcmA is the major autolysin of L. lactis; it is involved in cell separation after cell division and in cellular autolysis when cells reach the stationary phase (6). The Nterminal part of AcmA contains the catalytic domain, while the C-terminal part comprises three LysM domains involved in cell wall binding (33). AcmB, the second PGH of L. lactis, is built of three domains: an S/T/P/N-rich domain at its N terminus followed by the catalytic domain and a C-terminal part of unknown function. AcmB contributes to cellular autolysis to a lesser extent than AcmA and does not participate in cell separation (17). The third L. lactis PGH, AcmC, does not contain any specific cell wall binding domain an...

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Cloning and nucleotide sequence of the gene encoding the γ-?-glutamyl-?-diamino acid endopeptidase II of Bacillus sphaericus

Cited by 11 publications

References 7 publications

Analysis of the Peptidoglycan Hydrolase Complement of Lactococcus lactis : Identification of a Third N- Acetylglucosaminidase, AcmC

Analysis of the Peptidoglycan Hydrolase Complement of Lactococcus lactis : Identification of a Third N- Acetylglucosaminidase, AcmC

Isolation and characterisation of a 13.8-kDa bacteriolytic enzyme from house dust mite extracts: homology with prokaryotic proteins suggests that the enzyme could be bacterially derived

Lactococcus lactis Gene yjgB Encodes a γ- d -Glutaminyl- l -Lysyl- Endopeptidase Which Hydrolyzes Peptidoglycan

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