Purification and partial characterization of a 36-kDa chitinase from Bacillus thuringiensis subsp. colmeri, and its biocontrol potential

Liu, Dong; Cai, Jin; Xie, Chichu; Liu, Chuan; Chen, Yuehua

doi:10.1016/j.enzmictec.2009.10.007

Cited by 81 publications

(50 citation statements)

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“…Research on the regulatory mechanism of chitinase will permit better utilization of bacterial chitinase. Liu et al demonstrated that the chitinase produced by B. thuringiensis improved its insecticidal activity (9). Furthermore, the roles of CcpA and YvoA have been studied in some detail in B. subtilis compared to B. thuringiensis.…”

Section: Discussionmentioning

confidence: 99%

“…For chitinase gene expression assays, S minimal medium [15 (28) supplemented with 0.5% yeast extract powder, G medium (S medium plus 0.5% glucose), and C medium (S medium plus 0.5% colloidal chitin) were used. Colloidal chitin was prepared according to a previously described method (9). For strains with antibiotic resistance, appropriate antibiotics were added to the culture medium at the following concentrations: 5 g ml Ϫ1 chloramphenicol (Cam), 50 g ml Ϫ1 erythromycin (Erm), 50 g ml Ϫ1 ampicillin (Amp), and 50 g ml Ϫ1 kanamycin (Kan).…”

Section: Methodsmentioning

confidence: 99%

“…Bacillus thuringiensis (Bt) also produces chitinases (4)(5)(6). Several studies have reported that chitinases generated by Bt are involved in its antifungal activity and can enhance the insecticidal activity of Bt strains (7)(8)(9)(10). Many studies have reported the expression and application of chitinases in microorganisms (11)(12)(13)(14)(15).…”

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confidence: 99%

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YvoA and CcpA Repress the Expression of chiB in Bacillus thuringiensis

Jiang

Pan

et al. 2015

Appl Environ Microbiol

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c Bacillus thuringiensis produces chitinases, which are involved in its antifungal activity and facilitate its insecticidal activity. In our recent work, we found that a 16-bp sequence, dre chiB (AGACTTCGTGATGTCT), downstream of the minimal promoter region of the chitinase B gene (chiB) was a critical site for the inducible expression of chiB in B. thuringiensis Bti75. In this work, we show that a GntR family transcriptional regulator (named YvoA Bt ), which is homologous to YvoA of Bacillus subtilis, can specifically bind to the dre chiB oligonucleotide sequences in vitro by using electrophoretic mobility shift assays (EMSAs) and isothermal titration calorimetry (ITC) assays. The results of quantitative real-time reverse transcription-PCR (qRT-PCR) and Western blotting indicated that deletion of yvoA caused an ϳ7.5-fold increase in the expression level of chiB. Furthermore, binding of purified YvoA Bt to its target DNA could be abolished by glucosamine-6-phosphate (GlcN-6-P). We also confirmed, in the presence of the phosphoprotein Hpr-Ser 45 -P, that purified CcpA Bt bound specifically to the promoter of chiB, which contains the "cre chiB " sequence (ATAAAGCGTTTACA). According to the results of qRT-PCR and Western blotting, deletion of ccpA resulted in a 39-fold increase in the chiB expression level, and glucose no longer influenced the expression of chiB. We confirm that chiB is negatively controlled by both CcpA Bt and YvoA Bt in Bti75.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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YvoA and CcpA Repress the Expression of chiB in Bacillus thuringiensis

Jiang

Pan

et al. 2015

Appl Environ Microbiol

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“…Estas enzimas son responsables de la degradación de los principales polisacáridos que conforma la pared celular de hongos, mediante la hidrólisis de sus enlaces glucosídicos (Figura 5). Actualmente, existen diversos estudios científicos que reportan el papel de estas enzimas en la actividad antifúngica in vitro obtenidas de cepas del género Bacillus (Kishore et al, 2005;Liu et al, 2010;Shafi et al, 2017). Por ejemplo, Yan et al (2011) demostraron el papel de una quitinasa en el control de Rhizoctonia solani por B. subtilis SL-13, evaluando la actividad inhibitoria de la enzima purificada y confrontada contra dicho patógeno.…”

Section: Producción De Enzimas Líticasunclassified

El género Bacillus como agente de control biológico y sus implicaciones en la bioseguridad agrícola

Villarreal-Delgado

Villa-Rodríguez

Cira‐Chávez

et al. 2018

RMF

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Resumen. El género Bacillus se encuentra ampliamente distribuido en los agro-sistemas y una de sus principales aplicaciones es el control de enfermedades de cultivos agrícolas. En la presente revisión se describe y analiza al género Bacillus, y sus principales mecanismos de acción, tales como la excreción de antibióticos, toxinas, sideróforos, enzimas líticas e induciendo la resistencia sistémica, Abstract. The genus Bacillus is widely

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“…Dong Liu [20] and Muhammad Aamer Mehmood [21] found that CBP inhibited the spore germination of certain species of fungi. A chitin binding protein from Bacillus thuringiensis HD-1 has shown that this chitin binding protein is expressed in the spore mother cell and interacts with Cry1Ac to potentiate its insecticidal activity and facilitate the propagation of the bacillus strain in the environment by inhibiting the growth of certain fungi [22].…”

Section: Molecular Homology Modeling and Ligand Site Predictionmentioning

confidence: 99%

Three-dimensional (3D) structure prediction and function analysis of the chitin-binding domain 3 protein HD73_3189 from Bacillus thuringiensis HD73

Zhan

Guo

2015

BME

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Abstract. Bacillus thuringiensis (Bt) is capable of producing a chitin-binding protein believed to be functionally important to bacteria during the stationary phase of its growth cycle. In this paper, the chitin-binding domain 3 protein HD73_3189 from B. thuringiensis has been analyzed by computer technology. Primary and secondary structural analyses demonstrated that HD73_3189 is negatively charged and contains several α-helices, aperiodical coils and β-strands. Domain and motif analyses revealed that HD73_3189 contains a signal peptide, an N-terminal chitin binding 3 domains, two copies of a fibronectin-like domain 3 and a C-terminal carbohydrate binding domain classified as CBM_5_12. Moreover, analysis predicted the protein's associated localization site to be the cell wall. Ligand site prediction determined that amino acid residues GLU-312, TRP-334, ILE-341 and VAL-382 exposed on the surface of the target protein exhibit polar interactions with the substrate.

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Purification and partial characterization of a 36-kDa chitinase from Bacillus thuringiensis subsp. colmeri, and its biocontrol potential

Cited by 81 publications

References 30 publications

YvoA and CcpA Repress the Expression of chiB in Bacillus thuringiensis

YvoA and CcpA Repress the Expression of chiB in Bacillus thuringiensis

El género Bacillus como agente de control biológico y sus implicaciones en la bioseguridad agrícola

Three-dimensional (3D) structure prediction and function analysis of the chitin-binding domain 3 protein HD73_3189 from Bacillus thuringiensis HD73

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