DNA sequence of the Serratia marcescens lipoprotein gene
- 1 March 1980
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 77 (3) , 1369-1373
- https://doi.org/10.1073/pnas.77.3.1369
Abstract
The Serratia marcescens gene for the outer membrane lipoprotein (lpp) was cloned in λ phage vector Charon 14. The recombinant phage was very unstable, and the lpp gene with a 300-base-pair deletion at the transcription termination site was further cloned in pBR322. The DNA sequence of 834 base pairs encompassing the lpp gene was determined and compared with that of the Escherichia coli lpp gene. The sequence comparisons exhibit several unique features. (i) The promoter region is highly conserved (84% homology) and has an extremely high A+T content (78%) as in E. coli (80%). (ii) The 5′ nontranslated region of the lipoprotein mRNA is also highly conserved (95% homology). (iii) In the DNA sequence corresponding to the signal peptide of this secretory protein, there are three drastic changes, including addition of one base pair and deletion of four base pairs in S. marcescens as compared to E. coli. The resultant alterations in the amino acid sequence, however, do not change the basic properties of the signal peptide, which are assumed to be essential for its function in the secretory mechanism. (iv) The DNA sequence from the amino terminus to the 51st residue of the mature lipoprotein is highly conserved (95% homology) and there is no amino acid substitution. (v) The DNA sequence corresponding to the seven amino acid residues at the carboxyl terminus has only 42% homology, resulting in four amino acid substitutions. (vi) Within the section of 40 base pairs beginning with the termination codon (UAA) and ending immediately before the oligo(T) transcription termination site in the E. coli lpp gene, there is about 60% homology. However, after this section, there is no obvious homology between the two sequences, probably because of a deletion of 300 base pairs at this region. (vii) Seven stable stem-and-loop structures could be formed in the mRNA region. (viii) Alterations in the third position of codons used in the lpp gene suggest that the gene has evolved somewhat differently from other genes in S. marcescens.Keywords
This publication has 22 references indexed in Scilit:
- The Outer Membrane Proteins of Gram-Negative Bacteria: Biosynthesis, Assembly, and FunctionsAnnual Review of Biochemistry, 1978
- Homologous nucleotide sequences between prokaryotic and eukaryotic mRNAs: the 5'-end sequence of the mRNA of the lipoprotein of the Escherichia coli outer membrane.Proceedings of the National Academy of Sciences, 1978
- Charon Phages: Safer Derivatives of Bacteriophage Lambda for DNA CloningScience, 1977
- Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane.Proceedings of the National Academy of Sciences, 1977
- A new method for sequencing DNA.Proceedings of the National Academy of Sciences, 1977
- GENETIC RELATEDNESS IN THE FAMILY ENTEROBACTERIACEAEAnnual Review of Microbiology, 1976
- Nucleotide sequence of the rightward operator of phage lambda.Proceedings of the National Academy of Sciences, 1975
- Stability of ribonucleic acid double-stranded helicesJournal of Molecular Biology, 1974
- Improved Estimation of Secondary Structure in Ribonucleic AcidsNature New Biology, 1973
- Nonchromosomal Antibiotic Resistance in Bacteria: Genetic Transformation of Escherichia coli by R-Factor DNAProceedings of the National Academy of Sciences, 1972