Abstract
THE lipoprotein of Gram-negative bacteria has become a cell surface component of central interest following its characterisation by Braun and coworkers1. This small protein (molecular weight 7,500) is unique in containing as its N-terminal amino acid a glycerylcysteine to which three fatty acids are covalently bound2. It is also unusual in its subcellular distribution: one-third of the total lipoprotein is covalently linked to the cell wall peptidoglycan while the remaining two-thirds exists in an unlinked or “free” form in the outer membrane4. Free and murein-linked lipoprotein seem to be identical in structure5,6, and pulse–chase experiments indicate that free lipoprotein is the precursor to murein-linked lipoprotein4. Braun's lipoprotein or an immunologically related protein has been found in a wide variety of Gram-negative organisms7,8, and in Escherichia coli is present in about 3 × 105 copies per cell1. These observations suggest that lipoprotein performs some essential function(s); however, the nature of that function is unknown. It has been suggested that lipoprotein may have a role in anchoring the outer membrane to the cell wall3, or function in transporting small molecules through the outer membrane9 or be involved in cell division10,11. To clarify the role of Braun's lipoprotein, we have isolated a mutant deficient in its synthesis.
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TORTI, S., PARK, J. Lipoprotein of Gram-negative bacteria is essential for growth and division. Nature 263, 323–326 (1976). https://doi.org/10.1038/263323a0
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DOI: https://doi.org/10.1038/263323a0
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