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PMID: 3054490 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Comparison of the haemolysin secretion protein HlyB from Proteus vulgaris and Escherichia coli; site-directed mutagenesis causing impairment of export function.

Molecular & general genetics : MGG ·Vol. 213 ·No. 2-3 ·1988-08-00 ·Pages 551-5

Koronakis V, Koronakis E, Hughes C

Abstract

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.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/genetics,metabolism Base Sequence Carrier Proteins/genetics,metabolism DNA, Bacterial/genetics Escherichia coli/genetics,metabolism Genes, Bacterial Hemolysin Proteins Molecular Sequence Data Mutation Protein Kinases/genetics Proteus vulgaris/genetics,metabolism Sequence Homology, Nucleic Acid
Chemicals
Bacterial Proteins Carrier Proteins DNA, Bacterial Hemolysin Proteins Hlyb protein, Bacteria Protein Kinases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Koronakis V
Department of Pathology, Cambridge University, England.
Koronakis E
Hughes C
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Article Info
Journal
Molecular & general genetics : MGG
Abbr.
Mol Gen Genet
ISSN
0026-8925
DOI
10.1007/BF00339631
Published
1988-08-00
Pages
551-5
Language
English
Region
Germany
NLM ID
0125036
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00339631
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