Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation

Buist, G; Kok, J; Leenhouts, K J; Dabrowska, M; Venema, G; Haandrikman, A J

doi:10.1128/jb.177.6.1554-1563.1995

Cited by 247Bacterial Genetics and BiotechnologyProbiotics and Fermented FoodsBacteriophages and microbial interactions

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Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation

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Buist, G, Kok, J, Leenhouts, K J, Dabrowska, M, Venema, G, Haandrikman, A J·1995·Journal of Bacteriology

DOI 10.1128/jb.177.6.1554-1563.1995PMC PMC176772

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Abstract

A gene of Lactococcus lactis subsp. cremoris MG1363 encoding a peptidoglycan hydrolase was identified in a genomic library of the strain in pUC19 by screening Escherichia coli transformants for cell wall lysis activity on a medium containing autoclaved, lyophilized Micrococcus lysodeikticus cells. In cell extracts of L. lactis MG1363 and several halo-producing E. coli transformants, lytic bands of similar sizes were identified by denaturing sodium dodecyl sulfate (SDS)-polyacrylamide gels containing L. lactis or M. lysodeikticus cell walls. Of these clearing bands, corresponding to the presence of lytic enzymes with sizes of 46 and 41 kDa, the 41-kDa band was also present in the supernatant of an L. lactis culture. Deletion analysis of one of the recombinant plasmids showed that the information specifying lytic activity was contained within a 2,428-bp EcoRV-Sau3A fragment. Sequencing of part of this fragment revealed a gene (acmA) that could encode a polypeptide of 437 amino acid residues. The calculated molecular mass of AcmA (46,564 Da) corresponded to that of one of the lytic activities detected. Presumably, the enzyme is synthesized as a precursor protein which is processed by cleavage after the Ala at position 57, thus producing a mature protein with a size of 40,264 Da, which would correspond to the size of the enzyme whose lytic activity was present in culture supernatants of L. lactis. The N-terminal region of the mature protein showed 60% identity with the N-terminal region of the mature muramidase-2 of Enterococcus hirae and the autolysin of Streptococcus faecalis. Like the latter two enzymes, AcmA contains C-terminal repeated regions. In AcmA, these three repeats are separated by nonhomologous intervening sequences highly enriched in serine, threonine, and asparagine. Genes specifying identical activities were detected in various strains of L. lactis subsp. lactis and L. lactis subsp. cremoris by the SDS-polyacrylamide gel electrophoresis detection assay and PCR experiments. By replacement recombination, an acmA deletion mutant which grew as long chains was constructed, indicating that AcmA is required for cell separation.

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The properties of the mutant were in agreement with the anticipated features of the mutations.
“The properties of the mutant were in agreement with the anticipated features of the mutations (Tynkkynen et al., 1993; Buist et al., 1995; Kunji et al., 1995).”
From Reconstruction of the proteolytic pathway for use of β‐casein by Lactococcus lactis (1998) · cites this paper as Buist et al., 1995

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Self-citation

These include:
Buist, G., Kok, J., Leenhouts, K., Dabrowska, M., & Venema, G. (1994)
Self-citation
Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis
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Correspondence Marie-Pierre Chapot-Chartier
Lactis, L., Hansen, J., Foster, S. J., & Chapot, M.-P. (2002)
Cloning and Characterization of acmAas from Lactococcus lactis and Effect of a Truncated Derivative on Daughter-Cell Segregation and Growth
Li, L. (2009) · Huazhong Nongye Daxue xuebao
Analysis of the Peptidoglycan Hydrolase Complement of Lactococcus lactis : Identification of a Third N- Acetylglucosaminidase, AcmC
Huard‐Chauveau, C., Miranda, G., Redko, Y., Wessner, F., Foster, S. J., & Chapot‐Chartier, M. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.6.3493-3499.2004 · Cited by 43

Authors: Buist, G., Kok, J., Leenhouts, K. J., Dabrowska, M., Venema, G., & Haandrikman, A. J.
Affiliations: University of Groningen (NL)
Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Haren, The Netherlands.
ORCID: Buist, G
Kok, J
Haandrikman, A J
Venue: Journal of Bacteriology
Publisher: American Society for Microbiology
Published: 1995-03
Volume: 177
Issue: 6
Pages: 1554-1563
ISSN: 0021-9193 (ISSN-L)
1098-5530
DOI: 10.1128/jb.177.6.1554-1563.1995
PMC: PMC176772
OpenAlex: W2140544780
Cited by: 247
References: 53
Citations by year: 2026: 1 · 2025: 1 · 2024: 2 · 2023: 3 · 2022: 2 · 2021: 1 · 2020: 7 · 2019: 7 · 2018: 2 · 2017: 6 · 2016: 12 · 2015: 6 · 2014: 5 · 2013: 11 · 2012: 10
FWCI: 7.50
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Bacteriology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, other-oa)
Funders: Koninklijke Nederlandse Akademie van Wetenschappen
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
Life Sciences › Immunology and Microbiology › Virology › Bacteriophages and microbial interactions
Keywords: Lactococcus lactis, peptidoglycan hydrolase, lysozyme, cell wall lysis, cell isolation, autolysin, precursor protein processing, N-terminal sequence homology, Enterococcus hirae, Enterococcus faecalis, genomic library
MeSH terms: Amino Acid Sequence, Bacteriolysis, Base Sequence, Chromosomes, Bacterial, Cloning, Molecular, Escherichia coli, Genes, Bacterial, Molecular Sequence Data, Muramidase, Recombinant Proteins, Species Specificity, Lactococcus lactis, Restriction Mapping, Sequence Deletion, Sequence Homology, Amino Acid, Sequence Analysis, DNA

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Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation

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