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Expression and crystallization of an N-terminally activated form of the Bacillus thuringiensis Cry1Ca toxin.

journal contribution
posted on 2023-06-07, 23:08 authored by Thaleia Kouskoura, Candy Tickner, Neil CrickmoreNeil Crickmore
When the active form of the Bacillus thuringiensis delta-endotoxin Cry1Ca was expressed in E. coli severe growth retardation was observed. The absence of a short peptide from the N-terminus of the protoxin was responsible for this effect. The introduction of a mutation at an amino acid previously reported as being involved in the initial stages of pore formation within the natural insect target partially abolished the growth retardation effect. We suggest that removal of the N-terminal peptide is a necessary step in toxin activation, the presence of this peptide preventing proper interaction of the toxin with the target membrane. Expression of the truncated toxin in Bacillus thuringiensis also prevented the formation of Cry1Ca crystals.

History

Publication status

  • Published

Journal

Current Microbiology

ISSN

0343-8651

Issue

5

Volume

43

Page range

371-373

Pages

3.0

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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