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Extended screening by PCR for seven cry-group genes from field-collected strains of Bacillus thuringiensis
- E. Ben-Dov, A. Zaritsky, Y. Margalith
- Biology, MedicineApplied and environmental microbiology
- 1 December 1997
An extended multiplex PCR method was established to rapidly identify and classify Bacillus thuringiensis strains containing cry (crystal protein) genes toxic to species of Lepidoptera, Coleoptera and Diptera, thus facilitating subsequent toxicity assays.
Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases.
Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria
It is suggested that AHAS I enables a bacterium to cope with poor carbon sources, which lead to low endogenous pyruvate concentrations, and AHAS II and III are well suited to producing the branched-chain amino acid precursors during growth on glucose, they would fail to provide appropriate quantities of AL when the concentration of pyruVate is relatively low.
Multiplex PCR Screening To Detect cry9Genes in Bacillus thuringiensis Strains
- E. Ben-Dov, Qingfeng Wang, Y. Margalith
- Biology, MedicineApplied and Environmental Microbiology
- 1 August 1999
A set of universal (Un9) and specific primers for multiplex rapid screening for all four known genes from the cry9 group was designed and complements the existing PCR methodology for most currently known cry genes.
Coral mucus-associated bacterial communities from natural and aquarium environments.
- Netta Kooperman, E. Ben-Dov, E. Kramarsky-Winter, Z. Barak, A. Kushmaro
- Environmental Science, BiologyFEMS microbiology letters
- 1 November 2007
Comparisons of surface mucus microbiota of the coral Fungia granulosa from the natural environment with that from individuals maintained in aquaria suggest an adaptation of the mucus bacterial communities to the different conditions.
Isolation and characterization of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme.
It is suggested that the active sites of AHAS III are located at the interface of a dimer of catalytic subunits, and that such aDimer is not stable except in the presence of the small subunits.
Homology modeling of the structure of bacterial acetohydroxy acid synthase and examination of the active site by site-directed mutagenesis.
- M. Ibdah, A. Bar-Ilan, O. Livnah, J. Schloss, Z. Barak, D. Chipman
- Biology, ChemistryBiochemistry
- 17 December 1996
A model for the structure of Escherichia coli AHAS isozyme II, based on its homology with pyruvate oxidase and experimental testing of the model by site-directed mutagenesis, has been used here to study how AHAS controls the chemical fate of a decarboxylated keto acid.
Properties of subcloned subunits of bacterial acetohydroxy acid synthases
- O. Weinstock, C. Sella, D. Chipman, Z. Barak
- Biology, ChemistryJournal of bacteriology
- 1 September 1992
The catalytic machinery of these AHAS isozymes is entirely contained within the large subunits, and nearly all of the properties of the intact AHAS isozyme I or III can be reconstituted by mixing extracts containing the respective large and small subunits.
Structure of the regulatory subunit of acetohydroxyacid synthase isozyme III from Escherichia coli.