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The conserved cysteine residues in Bacillus thuringiensis Cry1Ac protoxin are not essential for the bipyramidal crystal formation.

08:00 EDT 27th March 2019 | BioPortfolio

Summary of "The conserved cysteine residues in Bacillus thuringiensis Cry1Ac protoxin are not essential for the bipyramidal crystal formation."

To evaluate the function of conserved cysteine residues in Cry1Ac protoxin, we constructed a series of Cry1Ac mutants in which single or multiple cysteine residues were replaced with serine. It was found that cysteine substitution had little effect on the protoxin expression and bipyramidal crystal formation. Bioassays using Plutella xylostella larvae showed that two mutants with fourteen cysteine residues in the C-terminal half and all sixteen residues replaced had similar toxicity as wildtype Cry1Ac protoxin. Our study suggests that the conserved cysteine resudues in the Cry1Ac protoxin are not essential for deposition into a bipyramidal crystal even though the C-terminal half was directly involved in crystal formation.

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Journal Details

This article was published in the following journal.

Name: Journal of invertebrate pathology
ISSN: 1096-0805
Pages: 82-85

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Medical and Biotech [MESH] Definitions

A family of proteins that are related to epidermal growth factor. They share in common a consensus sequence consisting of six spatially conserved CYSTEINE residues which form three intramolecular bonds. This consensus sequence is commonly referred to EGF motif and is considered essential for binding of the proteins to ERB RECEPTORS.

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A subfamily of ligand-gated ion channel receptors that share a characteristic loop which is formed by a disulfide bond between two CYSTEINE residues. These receptors typically contain five subunits with the cysteine-loop occurring near an N-terminal extracellular domain.

A proteoglycan family (SLRPs) that is defined by a central domain which consists of a variable number of repeats of the motif LXXLxLXXNxL, where L may be LEUCINE; ISOLEUCINE; VALINE; or other hydrophobic amino acids. The N-terminal contains four conserved CYSTEINE residues and may be modified depending on function. SLRPs provide structural support to the EXTRACELLULAR MATRIX and are critical for regulating its assembly and dynamics at CELL-MATRIX JUNCTIONS.

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