Abstract
A DNA sequence of 816 base pairs encompassing the entire Erwinia amylovora lipoprotein gene was determined. Sequence comparison between E. amylovora, Escherichia coli, and Serratia marcescens suggests that the structure of the lipoprotein has been highly conserved under the constraint of efficient gene expression selecting promoter structure, mRNA secondary structure, and codon usage in addition to the polypeptide function. The sequence also suggests that the lpp gene of the three bacteria diverged sequentially in the course of evolution.
Highlights
A DNA sequence of 816 base pairs encompassing the several interesting and unique featuroefs the Ipp genes which entire Erwinia amylovora lipoprotein gene was determined
The sequence suggests that the lpp gene of the three bacteria diverged sequentially in the course of evolution
Restriction enzymes were from Bethesda Research LaboraLipoprotein is a major outer membrane protein in Esche- tories and New England Biolabs
Summary
Sequence comparison between E. amylouom, Escherichia coli, and Serratia marcescens suggests that the structure of the lipoprotein has been highly conserved under the constraint of efficient gene expression are highly conserved in these bacteria. These features probably are relevant to the mechanisomf expression of the gene or the secretion and assembly of the lipoprotein into the outer membrane. The conservedregions wouldbeexpectedtoplayimportantrolesinthehighly efficient expressionof t h e lpp genes, inthe process of secretion and assembly of this protein into the outer membrane, or in 1100 plaques examined gave positive hybridization. Carried out only for parts of trp operon and the lpp region
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