The Lactococcus lactis sex‐factor aggregation gene cluA
Abstract
Summary: A gene, cluA, was cloned from the chromosomally located sex factor of Lactococcus lactis MG1363. Sequence analysis revealed significant homology with previously described aggregation proteins in Enterococcus and Streptococcus species. The possibility that cluA was an equivalent protein involved in cell aggregation between donor and recipient bacteria during lactococcal conjugation was confirmed by its expression under the control of a heterologous promoter in L. lactis. Analysis of the homology between the CluA protein and the related proteins of Enterococcus and Streptococcus allowed a common structure for these proteins to be postulated. This consisted of five domains. Functionally conserved domains I and V act respectively as a secretary leader and C‐terminal membrane anchor. Domains II and IV are conserved at the amino acid level and probably have common structural roles whereas domain III is variable and may control binding specificity.
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Concerning L. lactis, three surface proteins are attributed to the CWAP group: the chromosomally-encoded sex factor CluA, the plasmid-encoded proteinase NisP, and the plasmid-encoded cell serine proteinase PrtP.
“Concerning L. lactis, three surface proteins were attributed to the same group of CWAP: i) the chromosomally-encoded sex factor CluA [22], ii) the plasmid-encoded proteinase NisP [23], and iii) the plasmid-encoded cell serine proteinase PrtP (also called lactocepin [24], which initiates proteolytic degradation of milk casein [25]).”
From Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci (2007) · cites this paper as [22]
Two confirmed lactococcal proteins with cell wall anchor domains are the sex factor protein CluA and plasmid-encoded NisP, which is not present in MG1363.
“Two confirmed lactococcal proteins with cell wall anchor domains are the sex factor protein CluA [22], and plasmid-encoded NisP [23], which is not present in MG1363.”
From Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci (2007) · cites this paper as [22]
The CluA dependent cell aggregation phenotype is reportedly poorly expressed unless a co-integrate is formed between the sex factor and a lactose plasmid, so CluA is unlikely to be a significant adhesion factor in the experimental system.
“The CluA dependent cell aggregation phenotype is reportedly poorly expressed unless a co-integrate is formed between the sex factor and a lactose plasmid [22], so we consider it unlikely that CluA is a significant adhesion factor in our experimental system.”
From Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci (2007) · cites this paper as [22]
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“lactis, three surface proteins were attributed to the same group of CWAP: i) the chromosomally-encoded sex factor CluA [22], ii) the plasmidencoded proteinase NisP [23], and iii) the plasmidencoded cell serine proteinase PrtP (also called lactocepin [24], which initiates proteolytic degradation of milk casein [25]).”
BackgroundInfluential
- Authors
- Godon, J., Jury, K., Shearman, C. A., & Gasson, M. J.
- Affiliations
- Norwich Research Park (GB)
- Corresponding author
- Gasson, Michael J.
- ORCID
- Godon, Jean‐Jacques
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 1994-05
- Volume
- 12
- Issue
- 4
- Pages
- 655-663
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2168568850
- Cited by
- 50
- References
- 37
- Citations by year
- 2022: 2 · 2020: 1 · 2019: 2 · 2016: 1 · 2014: 3 · 2013: 1 · 2012: 1
- FWCI
- 2.53
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Institut National de la Recherche Agronomique
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Keywords
- Lactococcus lactis, sex factors, conjugation, cell aggregation, protein domain structure, Enterococcus, Streptococcus, protein secretion, membrane anchor, binding specificity, gene cloning
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, Base Sequence, Cloning, Molecular, Conjugation, Genetic, F Factor, Genes, Bacterial, Molecular Sequence Data, Lactococcus lactis, Gene Expression, Sequence Homology, Amino Acid, DNA Primers
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