✦ LIBER ✦
Comparison of the haemolysin secretion protein HlyB from Proteus vulgaris and Escherichia coli; site-directed mutagenesis causing impairment of export function
✍ Scribed by Koronakis, Vassilis ;Koronakis, Eva ;Hughes, Colin
- Publisher
- Springer
- Year
- 1988
- Tongue
- English
- Weight
- 470 KB
- Volume
- 213
- Category
- Article
- ISSN
- 0026-8925
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✦ Synopsis
The hlyB secretion genes of Proteus vulgaris and Escherichia coli showed 81% nucleotide homology and similar E. coli-atypical codon usage. The deduced protein sequences differed in 54 of 707 residues and shared a previously unreported sequence which corresponds to the ATP-binding motif characteristic of protein kinases. The motif was also conserved in the HlyB of Morganella morganii. Of 4 oligonucleotide-directed substitutions introduced into the putative E. coli HlyB motif, 2 non-conservative changes caused radical reductions in the export of active haemolysin protein.