The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
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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Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572
Detection of specific sequences among DNA fragments separated by gel electrophoresis
Southern, E. M. (1975) · Journal of Molecular Biology · doi:10.1016/s0022-2836(75)80083-0 · Cited by 32,245
A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
Feinberg, A. P., & Vogelstein, B. (1983) · Analytical Biochemistry · doi:10.1016/0003-2697(83)90418-9 · Cited by 24,512
A comprehensive set of sequence analysis programs for the VAX
Devereux, J., Haeberli, P. E., & Smithies, O. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.1part1.387 · Cited by 14,222
A new method for predicting signal sequence cleavage sites
von HEIJNE, G. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.11.4683 · Cited by 4,473
Rapid transfer of DNA from agarose gels to nylon membranes
Reed, K. C., & Mann, D. A. (1985) · Nucleic Acids Research · doi:10.1093/nar/13.20.7207 · Cited by 1,731
Chung, C. T., Niemelä, S., & Miller, R. H. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.7.2172 · Cited by 1,602
Catabolic repression of bacterial sporulation.
Schaeffer, P., Millet, J., & Aubert, J.-M. (1965) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.54.3.704 · Cited by 1,185
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Terpe, K. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-006-0465-8 · Cited by 1,039
“All known extracellular proteases are deficient in the strain WB800 ( Margot and Karamata 1996 ).”
BackgroundTjalsma, H., Bolhuis, A., Jongbloed, J. D. H., Bron, S., & van Dijl, J. M. (2000) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.64.3.515-547.2000 · Cited by 806
“subtilis, proteins retained in the cell wall include DNases, RNases (173), proteases (10, 163, 274), enzymes involved in the synthesis of peptidoglycan (penicillin-binding proteins), and cell wall hydrolases (20, 96, 97) that are involved in cell wall turnover during cell growth, cell division, sporulation, and germin…”
BackgroundProteomics of Protein Secretion by Bacillus subtilis : Separating the “Secrets” of the Secretome
Tjalsma, H., Antelmann, H., Jongbloed, J. D. H., Braun, P. G., Darmon, E., Dorenbos, R., Dubois, J. F., Westers, H., Zanen, G., Quax, W. J., et al. (2004) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.68.2.207-233.2004 · Cited by 581
“HtrA, HtrB (85), and WprA (68, 124) are involved in the quality control of secretory proteins.”
BackgroundInfluentialWesters, L., Westers, H., & Quax, W. J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.02.011 · Cited by 491
A Proteomic View on Genome-Based Signal Peptide PredictionsPreprint
Antelmann, H., Tjalsma, H., Voigt, B., Ohlmeier, S., Bron, S., van Dijl, J. M., & Hecker, M. (2001) · Genome Research · doi:10.1101/gr.182801 · Cited by 359
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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