Bacterial ‘histone‐like protein I’ (HLP‐I) is an outer membrane constituent?

FEBS Letters

Koski, Pertti²  Hirvas, Laura²  Coleman, Jack¹  Vaara, Martti² 

[1] Department of Biochemistry and Molecular Biology, Louisiana State University Medical Center, New Orleans, LA 70112, USA;Department of Bacteriology and Immunology, University of Helsinki, 00290 Helsinki, Finland

关键词: ompH gene;    hlpA gene;    Outer membrane protein;    DNA binding protein;    Bacterial chromatid;    (Escherichia coli;    Salmonella typhimurium);    aa;    amino acid(s);    LPS;    lipopolysaccharide;    nt;    nucleotide(s);    OM;    outer membrane;    ORF;    open reading frame;   

DOI  :  10.1016/0014-5793(90)80169-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown