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The wprA gene of Bacillus subtilis 168, expressed during exponential growth, encodes a cell-wall-associated protease
Abstract
The nucleotide sequence of wprA, a protease-encoding gene of Bacillus subtilis 168, is reported. The gene, expressed during the exponential growth phase, belongs to a monocistronic operon. WprA is a 96 kDa polypeptide endowed with a signal peptide, as well as a propeptide. Upon processing and export, it gives rise to two previously identified cell-wall-bound proteins, CWBP23 and 52. Processing of WprA exhibits a novel feature of protein export, whereby removal of the middle part of the molecule accompanies the targeting to the cell wall of its N- and C-terminal parts, which correspond to CWBP23 and 52, respectively. Sequence analyses and enzymic assays reveal that CWBP52 is a serine protease. Growth rate, cell morphology, sporulation and motility of wprA mutants apparently do not differ from those of the parent strain.
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“Taken together, our results suggest that the mechanism of PrtB attachment to the cell wall probably implicates electrostatic forces, as was proposed for WprA, a cell wall-associated protease of Bacillus subtilis (24).”
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“All known extracellular proteases are deficient in the strain WB800 ( Margot and Karamata 1996 ).”
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“Complex arrays of proteases are also found in numerous other bacteria, using both genetic and sequence analyses (Pero and Sloma, 1993; WuÈlfing and PluÈckthun, 1994; Gottesman, 1996; Margot and Karamata, 1996; Koonin et al., 1997; Pallen and Wren, 1997).”
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“Therefore, spot J was CWBP52 serine protease and spot C4 was CWBP23 (Margot & Karamata, 1996; Stephenson & Harwood, 1998).”
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“Third, the membrane-cell wall interface contains numerous proteases, such as the wprA-encoded CWBP52 (20, 34) and homologues of the E. coli HtrA and Tsp proteases (our unpublished observations), which appear to play a role in the quality control of secreted proteins.”
BackgroundThe ins and outs of Bacillus proteases: activities, functions and commercial significance
Harwood, C. R., & Kikuchi, Y. (2021) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuab046 · Cited by 116
The Bacillus subtilis cannibalism toxin SDP collapses the proton motive force and induces autolysis
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“…lytF::spec, lytE::cm lytD::tet PY79 This study HB0020 DsigW::mls trpC2 DSPb 168 Cao et al. (2001) L16601 Prototrophic derivative of B. subtilis 168 Margot and Karamata (1996) L16648 lytABC::neo, lytF::spec, lytE::cm, lytD::tet L16601 Margot et al. (1999) CDE433 DsdpABCIR::tet, DsigW::kan PY79…”
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“The resulting plasmid was used to transform strain L16601 to chloramphenicol resistance (17).”
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Miyoshi, A., Poquet, I., Azevedo, V., Commissaire, J., Bermúdez‐Humarán, L. G., Domakova, E., Loir, Y. L., Oliveira, S. C., Gruss, A., & Langella, P. (2002) · Applied and Environmental Microbiology · doi:10.1128/aem.68.6.3141-3146.2002 · Cited by 95
Influence of a Cell-Wall-Associated Protease on Production of α-Amylase by Bacillus subtilis
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“One such protease is CWBP52, a processed product of the wprA gene, that has been shown to be bound noncovalently to the cell wall (21).”
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“B. subtilis strain L16601 (wild-type strain, Margot and Karamata, 1996) was used as indicator and propagation host for SPP1wt (Riva et al., 1968) and SPP1mut phages.”
MethodHyyryläinen, H., Marciniak, B. C., Dahncke, K., Pietiäinen, M., Courtin, P., Vitikainen, M., Seppälä, R., Otto, A., Becher, D., Chapot‐Chartier, M., et al. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07188.x · Cited by 73
“…proteins There are several ‘periplasmic’ proteases which could be involved in the quality control and degradation of PBPs including HtrA, HtrB, PrsW and WprA (Margot and Karamata, 1996; Stephenson and Harwood, 1998; Hyyryläinen et al., 2001; Ellermeier and Losick, 2006; Heinrich et al., 2008).”
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Assembly of Minicellulosomes on the Surface of Bacillus subtilis
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Erskine, E., Morris, R. J., Schor, M., Earl, C., Gillespie, R. M. C., Bromley, K. M., Sukhodub, T., Clark, L., Fyfe, P. K., Serpell, L. C., et al. (2018) · Molecular Microbiology · doi:10.1111/mmi.13985 · Cited by 48
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“Among them are WprA protease, wall-associated protein WapA and autolysins ( Margot & Karamata, 1996; Smith et al., 2000; Yoshida et al., 1995).”
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van Tilburg, A. Y., van Heel, A. J., Stülke, J., de Kok, N. A. W., Rueff, A.-S., & Kuipers, O. P. (2020) · ACS Synthetic Biology · doi:10.1021/acssynbio.0c00194 · Cited by 41
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“wprA codes for a 96-kDa protein that is processed to the CWBP23 propeptide and CWBP52 mature protease, forming a complex associated with the cell wall (14).”
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“Taken together, our results suggest that the mechanism of PrtB attachment to the cell wall probably implicates electrostatic forces, as was proposed for WprA, a cell wall-associated protease of Bacillus subtilis (24).”
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“The minor extracellular proteases include Epr (2, 27), bacillopeptidase F (Bpr) (30, 31, 39), metalloprotease (Mpr) (20, 23, 28), neutral protease B (NprB) (35), wall-associated extracellular protease (WprA) (17), and Vpr (29).”
BackgroundCodY Regulates Expression of the Bacillus subtilis Extracellular Proteases Vpr and Mpr
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Accumulation of an artificial cell wall-binding lipase by Bacillus subtilis wprA and/or sigD mutants
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Host Organisms:Bacillus subtilis
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Protein Transport Pathways inBacillus subtilis: a Genome-Based Road Map
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Development of a LytE‐based high‐density surface display system in Bacillus subtilis
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“Others include a wall-bound protease WprA (Margot and Karamata, 1996), a major wallassociated protein WapA with unknown functions (Foster, 1993) and several less well-characterized wall-associated proteins.”
García‐Moyano, A., Larsen, Ø., Gaykawad, S. S., Christakou, E., Boccadoro, C., Puntervoll, P., & Bjerga, G. E. K. (2020) · Applied and Environmental Microbiology · doi:10.1128/aem.02090-20 · Cited by 20
“The strain KO7, however, still carries the gene wprA, which encodes a quality control exopeptidase that is constitutively expressed during vegetative growth (9) and known to be functional at the wall-membrane interface or in the wall itself, rather than being secreted into the culture medium (10).”
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Simultaneous Display of Bacterial and Fungal Lipases on the Cell Surface of Bacillus subtilis.
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Production of a recombinant lipase artificially localized on theBacillus subtiliscell surface
Tsuchiya, A., Kobayashi, G., Yamamoto, H., & Sekiguchi, J. (1999) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1999.tb13686.x · Cited by 14
“Margot and Karamata reported that wprA encodes a cell wallassociated protease [20].”
BackgroundFernandes, S., Labarde, A., Baptista, C., Jakutytè, L., Tavares, P., & São‐José, C. (2016) · Virology · doi:10.1016/j.virol.2016.05.004 · Cited by 12
Salt stress represses production of extracellular proteases in Bacillus pumilus
Liu, R. F., Huang, C., & Feng, H. (2015) · Genetics and Molecular Research · doi:10.4238/2015.may.11.27 · Cited by 11
“subtilis 168 (Margot and Karamata, 1996), seemed not to be affected by salt stress, especially in the early and mid-stationary growth phases (Figure 4).”
BackgroundProteases HtrA and HtrB for α-amylase secreted from Bacillus subtilis in secretion stress
Yan, S., & Wu, G. (2019) · Cell Stress and Chaperones · doi:10.1007/s12192-019-00985-1 · Cited by 10
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“Upon processing and export, it is also converted into two cell-wall-bound proteins, CWBP23 and 52 [10].”
BackgroundMulti-domain, cell-envelope proteinases of lactic acid bacteria
Siezen, R. J. (1999) · Springer eBooks · doi:10.1007/978-94-017-2027-4_6 · Cited by 14
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Identification of Laboratory-Specific Variations ofBacillus subtilisStrains Used in Japan
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“In addition, a deletion mutation in the epr gene resulted in low protease activity in the culture supernatant. wprA encodes a 96-kDa protein that is processed to the CWBP23 propeptide and CWBP52 mature protease, forming a complex associated with the cell wall (Margot et al., 1996).”
Sequencing of regions downstream of addA (98°) and citG (28°) in Bacillus subtilis
Medina, N., Vannier, F., Roche, B., Autret, S., Lévine, A., & Séror, S. J. (1997) · Microbiology · doi:10.1099/00221287-143-10-3305 · Cited by 5
Sinsuwan, S., Rodtong, S., & Yongsawatdigul, J. (2011) · Journal of Food Science · doi:10.1111/j.1750-3841.2011.02058.x · Cited by 4
“lactis NCDO 763 showed molecular mass of 19, 52, and 80 kDa, respectively (Monnet and others 1987; Fricke and others 2001; Margot and Karamata 1996).”
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Production of a recombinant lipase artificially localized on the Bacillus subtilis cell surface
Tsuchiya, A. (1999) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(99)00263-3 · Cited by 3
Proteomics of protein secretion by Bacillus subtilis
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ZYMOGRAPHY OF EXTRACELLULAR PROTEASES IN Bacillus subtilis
Kodama, T., Endo, K., Ara, K., Ozaki, K., & Sekiguchi, J. (2013) · Cited by 2
Optimisation of feedstock utilisation by Geobacillus thermoglucosidasius
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A comparative study of native and heterologous enzyme production in Bacillus subtilis
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Osamura, T., Takahashi, F., Endo, K., Okuda, M., & Takimura, Y. (2023) · Biochemical Engineering Journal · doi:10.1016/j.bej.2023.108996 · Cited by 1
Recombinant Glycoenzyme Production in Gram-Positive Bacteria—An Overview
Mohseni, A. H., Taghinezhad‐S, S., & Voglmeir, J. (2020) · Trends in Glycoscience and Glycotechnology · doi:10.4052/tigg.1824.1e · Cited by 1
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Metadata
- Authors
- Margot, P., & Karamata, D.
- Affiliations
- University of Lausanne (CH)
- Corresponding author
- Karamata, D.
- Venue
- Microbiology
- Publisher
- Microbiology Society
- Published
- 1996-12-01
- Volume
- 142
- Issue
- 12
- Pages
- 3437-3444
- ISSN
- 1350-0872 (ISSN-L)
- 1465-2080
- OpenAlex
- W2119045079
- Cited by
- 107
- References
- 36
- Citations by year
- 2023: 2 · 2022: 2 · 2021: 2 · 2020: 5 · 2019: 5 · 2018: 2 · 2017: 3 · 2016: 3 · 2015: 4 · 2014: 5 · 2013: 5 · 2012: 3
- FWCI
- 3.20
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Microbiology (publishedVersion)
- PubMed (publishedVersion)
- IRIS (submittedVersion)
- SERVAL (Université de Lausanne) (submittedVersion)
- Funders
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- Bacillus subtilis 168, serine protease, protein export, signal peptide, propeptide processing, exponential growth, gene sequence
- MeSH terms
- Amino Acid Sequence, Bacillus subtilis, Bacterial Proteins, Base Sequence, Binding Sites, Cell Wall, Cloning, Molecular, Genes, Bacterial, Molecular Sequence Data, Operon, Endopeptidases, Recombinant Proteins, Serine Endopeptidases, Subtilisins, Restriction Mapping, Gene Expression Regulation, Bacterial, Gene Expression Regulation, Enzymologic, Conserved Sequence, Sequence Homology, Amino Acid
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