Bacterial ‘histone‐like protein I’ (HLP‐I) is an outer membrane constituent?
- 12 March 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 262 (1), 123-126
- https://doi.org/10.1016/0014-5793(90)80169-j
Abstract
The nucleoid‐associated ‘histone‐like protein I’ (HLP‐I) protein of E. coli was found to be homologous with the cationic 16‐kDa outer membrane protein OmpH of Salmonella typhimurium. Deduced from the nucleotide sequence, the HLP‐I protein has 91% identical residues with the OmpH protein. Both proteins have very similar cleavable signal sequences. The nucleotide sequence similarity between the corresponding genes hlpA and ompH is 87%. The ompH gene is located in a gene cluster resembling the hlpA‐ORF17 region of E. coli which is close to the Ipx genes involved in the biosynthesis of lipopolysaccharides. The localization of the OmpH/HLP‐I protein in the cell is discussed.Keywords
This publication has 19 references indexed in Scilit:
- Unity in Function in the Absence of Consensus in Sequence: Role of Leader Peptides in ExportScience, 1989
- Identity of the 17-kilodalton protein, a DNA-binding protein from Escherichia coli, and the firA gene productJournal of Bacteriology, 1988
- Cloning and sequencing of the gene for the DNA-binding 17 K protein of Escherichia coliGene, 1988
- Purification and characterization of the 17 K protein, a DNA-binding protein from Escherichia coliBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- DNA- and RNA-binding proteins of chromatin from Escherichia coliBiochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1987
- [9] Nick translationMethods in Enzymology, 1987
- Dideoxy sequencing method using denatured plasmid templatesAnalytical Biochemistry, 1986
- PROTEIN SECRETION IN ESCHERICHIA COLIAnnual Review of Microbiology, 1985
- Prokaryotic histone-like protein interacting with RNA polymerase.Proceedings of the National Academy of Sciences, 1980
- DNA sequencing with chain-terminating inhibitorsProceedings of the National Academy of Sciences, 1977