Hyperproduction of chitinase influences crystal toxin synthesis and sporulation of Bacillus thuringiensis View Full Text


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Article Info

DATE

2009-04-01

AUTHORS

J. Eleazar Barboza-Corona, Tomás Ortiz-Rodríguez, Norma de la Fuente-Salcido, Dennis K. Bideshi, Jorge E. Ibarra, Rubén Salcedo-Hernández

ABSTRACT

Bacillus thuringiensis HD-73 was transformed with the endochitinase gene chiA74 under the control of a strong promoter (pcytA) and a 5′ mRNA stabilizing (STAB-SD) sequence (HD-73-pEBchiA74). Expression levels were compared with those observed from the wild type strain (HD-73) and the recombinant HD-73 strain expressing chiA74 under the control of its native promoter (HD-73-pEHchiA74). The chitinolytic activity of HD-73-pEBchiA74 was markedly elevated, being ~58- and 362-fold higher than, respectively, HD-73-pEHchiA74 and parental HD-73, representing the highest levels of chitinase expression in recombinant B. thuringiensis reported to date. Parasporal crystals measured under transmission electron microscopy showed that HD-73 produced crystals of 1.235 (±0.214) and 1.356 (±0.247) μm in length when the bacterium was grown in respectively, NBS and NBS with glucose. Otherwise, HD-73-pEBchiA74 synthesized crystals of 1.250 (±0.222) and 1.139 (±0.202) μm in length when cultivated in NBS and NBS with glucose, respectively, values that showed a diminution of ~10 and 20% compared with crystals produced by HD-73-pEHchiA74 grown under the same conditions. Comparison of viable spore counts per ml showed that HD-73-pEBchiA74 produced fewest viable spores (1.5 × 109, 1.3 × 109), compared to HD-73-pEHchiA74 (4.9 × 109, 5.3 × 109) and HD-73 (6.8 × 109, 8.8 × 109) when grown in NBS and NBS supplemented with glucose, respectively. No change in cellular protease activity was observed despite the overproduction of the chitinase. More... »

PAGES

31-42

References to SciGraph publications

  • 2007-12-14. Molecular and Biochemical Characterization of an Endochitinase (ChiA-HD73) from Bacillus thuringiensis subsp. kurstaki HD-73 in MOLECULAR BIOTECHNOLOGY
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  • 1999-12. Selection of chitinolytic strains of Bacillus thuringiensis in BIOTECHNOLOGY LETTERS
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  • 2001-08. Chitinase from Bacillusthuringiensis subsp. pakistani in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • 2008-02-08. Improving the Insecticidal Activity by Expression of a Recombinant cry1Ac Gene with Chitinase-Encoding Gene in Acrystalliferous Bacillus thuringiensis in CURRENT MICROBIOLOGY
  • 1999-04. Selection and characterization of a proteo-chitinolytic strain of Bacillus thuringiensis, able to grow in shrimp waste media in WORLD JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
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  • 2005-10. Molecular cloning and purification of an endochitinase from Serratia marcescens (Nima) in MOLECULAR BIOTECHNOLOGY
  • 2007-06-26. The 20-kDa Protein of Bacillus thuringiensis subsp. israelensis Enhances Bacillus sphaericus 2362 Bin Toxin Synthesis in CURRENT MICROBIOLOGY
  • 2001-01. Construction of protein overproducer strains in Bacillus subtilis by an integrative approach in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • 2006-11-30. Development of a recombinant strain of Bacillus thuringiensis subsp. kurstaki HD-73 that produces the endochitinase ChiA74 in ANTONIE VAN LEEUWENHOEK
  • 1970-08. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 in NATURE
  • 2008-08-20. Kinetics of Bacillus thuringiensis var. israelensis growth on high glucose concentrations in JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY
  • 2004-03. Expression of Chitinase-Encoding Genes in Bacillus thuringiensis and Toxicity of Engineered B. thuringiensis subsp. aizawai Toward Lymantria dispar Larvae in CURRENT MICROBIOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s10482-009-9332-9

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    http://dx.doi.org/10.1007/s10482-009-9332-9

    DIMENSIONS

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    PUBMED

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    32 schema:description Bacillus thuringiensis HD-73 was transformed with the endochitinase gene chiA74 under the control of a strong promoter (pcytA) and a 5′ mRNA stabilizing (STAB-SD) sequence (HD-73-pEBchiA74). Expression levels were compared with those observed from the wild type strain (HD-73) and the recombinant HD-73 strain expressing chiA74 under the control of its native promoter (HD-73-pEHchiA74). The chitinolytic activity of HD-73-pEBchiA74 was markedly elevated, being ~58- and 362-fold higher than, respectively, HD-73-pEHchiA74 and parental HD-73, representing the highest levels of chitinase expression in recombinant B. thuringiensis reported to date. Parasporal crystals measured under transmission electron microscopy showed that HD-73 produced crystals of 1.235 (±0.214) and 1.356 (±0.247) μm in length when the bacterium was grown in respectively, NBS and NBS with glucose. Otherwise, HD-73-pEBchiA74 synthesized crystals of 1.250 (±0.222) and 1.139 (±0.202) μm in length when cultivated in NBS and NBS with glucose, respectively, values that showed a diminution of ~10 and 20% compared with crystals produced by HD-73-pEHchiA74 grown under the same conditions. Comparison of viable spore counts per ml showed that HD-73-pEBchiA74 produced fewest viable spores (1.5 × 109, 1.3 × 109), compared to HD-73-pEHchiA74 (4.9 × 109, 5.3 × 109) and HD-73 (6.8 × 109, 8.8 × 109) when grown in NBS and NBS supplemented with glucose, respectively. No change in cellular protease activity was observed despite the overproduction of the chitinase.
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