Cloning, genetic organization, and characterization of a structural gene encoding bacillopeptidase F from Bacillus subtilis.

Wu, Xiaodong; Nathoo, S.; Pang, Andrew; Carne, T. K.; Wong, Sui‐Lam

doi:10.1016/s0021-9258(19)39225-7

Cited by 69 publications

(4 citation statements)

References 39 publications

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“…Other Methods-All PCRs were carried out using Vent polymerase (New England Biolabs). The PCR conditions, plasmid isolation, DNA transformation, Western blotting, and nucleotide sequencing were performed as described previously (28,29). The concentration of purified streptavidin was determined spectrophotometrically using a molar extinction coefficient of 41,820 M Ϫ1 cm Ϫ1 at 280 nm (30) for streptavidin.…”

Section: Table Imentioning

confidence: 99%

Development and Characterization of a Series of Soluble Tetrameric and Monomeric Streptavidin Muteins with Differential Biotin Binding Affinities

Qureshi¹,

Yeung²,

et al. 2001

Journal of Biological Chemistry

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The strong biotin-streptavidin interaction limits the application of streptavidin as a reversible affinity matrix for purification of biotinylated biomolecules. To address this concern, a series of single, double, and triple streptavidin muteins with different affinities to biotin were designed. The strategy involves mutating one to three strategically positioned residues (Ser-45, Thr-90, and Asp-128) that interact with biotin and other framework structure-maintaining residues of streptavidin. The muteins were produced in soluble forms via secretion from Bacillus subtilis. The impact of individual residues on the overall structure of streptavidin is reflected by the formation of monomeric streptavidin to different extents. Of the three targeted residues, Asp-128 has the most dramatic effect (Asp-128 > Thr-90 > Ser-45). Conversion of all three targeted residues to alanine results in a soluble biotin binding mutein that exists 100% in the monomeric state. Both wild-type and mutated (monomeric and tetrameric) streptavidin proteins were purified, and their kinetic parameters (on- and off-rates) were determined using a BIAcore biosensor with biotin-conjugated bovine serum albumin immobilized to the sensor chip. This series of muteins shows a wide spectrum of affinity toward biotin (K(d) from 10(-6) to 10(-11) m). Some of them have the potential to serve as reversible biotin binding agents.

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Section: Table Imentioning

confidence: 99%

Development and Characterization of a Series of Soluble Tetrameric and Monomeric Streptavidin Muteins with Differential Biotin Binding Affinities

Qureshi¹,

Yeung²,

et al. 2001

Journal of Biological Chemistry

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“…These enzymes are expressed at the beginning of the stationary phase in B. subtilis . Inactivation of their encoding genes does not affect either vegetative growth or sporulation, and they probably function as scavenging enzymes to supply the cell with amino acids derived from protein degradation [ 32 ].…”

Section: Discussionmentioning

confidence: 99%

Biodegradation of Pine Processionary Caterpillar Silk Is Mediated by Elastase- and Subtilisin-like Proteases

Diez-Galán

Cobos

Ibáñez

et al. 2022

IJMS

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Pine processionary caterpillar nests are made from raw silk. Fibroin protein is the main component of silk which, in the case of pine processionary caterpillar, has some unusual properties such as a higher resistance to chemical hydrolysis. Isolation of microorganisms naturally present in silk nests led to identification of Bacillus licheniformis and Pseudomonas aeruginosa strains that in a defined minimal medium were able to carry out extensive silk biodegradation. A LasB elastase-like protein from P. aeruginosa was shown to be involved in silk biodegradation. A recombinant form of this protein expressed in Escherichia coli and purified by affinity chromatography was able to efficiently degrade silk in an in vitro assay. However, silk biodegradation by B. licheniformis strain was mediated by a SubC subtilisin-like protease. Homologous expression of a subtilisin Carlsberg encoding gene (subC) allowed faster degradation compared to the biodegradation kinetics of a wildtype B. licheniformis strain. This work led to the identification of new enzymes involved in biodegradation of silk materials, a finding which could lead to possible applications for controlling this pest and perhaps have importance from sanitary and biotechnological points of view.

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“…Eight extracellular proteases have been identified in B. subtilis to date, which are encoded by the following genes: aprE (Stahl et al, 1984;Wong et al, 1984), bpr (Sloma et al, 1990b;Wu et al, 1990), epr (Bruckner et al, 1990;Sloma et al, 1988), mpr (Rufo et al, 1990;Sloma et al, 1990a), nprB (Tran et al, 1991), nprE (Yang et al, 1984), vpr (Sloma et al, 1991), and wprA (Margot et al, 1996). Deletions in the aprE (encoding subtilisin, alkaline protease) and nprE (encoding neutral protease) genes were the first such mutations, whose mutants show lower activities of extracellular proteases (Sloma et al, 1991).…”

Section: Inhibition Of Proteolysis Of Heterologous and Nature Proteins After The Translocation Process By Inactivation Of Multiple Proteamentioning

confidence: 99%

Advances in Applied Biotechnology

Zhang¹,

Nakajima²

2015

Lecture Notes in Electrical Engineering

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in 1981. He worked as a microbiologist at the National Institute of R&D in Floriculture, as a research assistant, and as a principal investigator at R&D Institute for Vegetables and Fruits Processing. He has also been acting as a lecturer at the Ecological University of Bucharest and worked as a senior researcher at the National Institute for R&D in Horticultural Biotechnology Stefanesti-Arges. Since 2007, he has been teaching as a professor of biotechnology for environmental protection, microbiology and bioremediation at the University of Pitesti, Faculty of Sciences. So far, he wrote and published over 140 papers, 50 of them being published in international journals and proceeding volumes all over the world; he published 10 books in Romania and had 2 book chapters published by Marcel Dekker and Kluwer Academic Publishers. During the last decade, he registered, as first author, 10 Romanian patents in the field of biotechnology for edible and medicinal mushroom cultivation and has been awarded with gold and silver medals at international exhibitions for inventions, research and new technologies. Contents Preface XI Part Biotechnology of Agricultural Wastes -Recycling, Saving Energy and Food Quality Preservation 1 Chapter Biotechnology of Agricultural Wastes Recycling Through Controlled Cultivation of Mushrooms 3

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Cloning, genetic organization, and characterization of a structural gene encoding bacillopeptidase F from Bacillus subtilis.

Cited by 69 publications

References 39 publications

Development and Characterization of a Series of Soluble Tetrameric and Monomeric Streptavidin Muteins with Differential Biotin Binding Affinities

Development and Characterization of a Series of Soluble Tetrameric and Monomeric Streptavidin Muteins with Differential Biotin Binding Affinities

Biodegradation of Pine Processionary Caterpillar Silk Is Mediated by Elastase- and Subtilisin-like Proteases

Advances in Applied Biotechnology

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