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Bacterial ‘histone‐like protein I’ (HLP‐I) is an outer membrane constituent?
Author(s) -
Hirvas Laura,
Coleman Jack,
Koski Pertti,
Vaara Martti
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80169-j
Subject(s) - biology , bacterial outer membrane , nucleic acid sequence , biochemistry , peptide sequence , gene , nucleoid , histone , microbiology and biotechnology , escherichia coli
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 ‐ORF 17 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.