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Chapter 4 : Structure, Function, and Transport of Lipoproteins in

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Structure, Function, and Transport of Lipoproteins in , Page 1 of 2

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Abstract:

In , lipoproteins are anchored to the periplasmic side of either the inner or outer membrane depending on the lipoprotein-sorting signal. Some gram-negative bacteria are known to possess lipoproteins on the outer surface of their outer membranes. The author and coresearchers therefore determined their N-terminal sequences and found that these three proteins are processed to nonlipidated mature forms, indicating that the three genes do not encode lipoproteins. Only two lipoproteins, LolB and YfiO, were essential as reported. They overproduced each of the 90 lipoproteins and examined the level of degP expression. To discuss the molecular mechanisms underlying lipoprotein sorting, one must understand the functions of the Lol pathway mediating the inner to outer membrane transport of lipoproteins. LolCDE and MsbA are two essential ABC transporters that appear to be involved in the biogenesis of the envelope. To evaluate lipoprotein-sorting signals, the LolA-dependent release of lipoproteins from spheroplasts was examined. Therefore, LolCDE only recognizes an N-terminal Cys possessing three acyl chains, the sole common structure of lipoproteins. The Lol avoidance mechanism is required for the localization of PulA of on the outer surface of the outer membrane. , the Lyme disease spirochete, has been reported to possess more than 100 lipoproteins, some of which are on the outer surface of the outer membrane and cause an immunoresponse of host cells.

Citation: Tokuda H, Matsuyama S, Tanaka-Masuda K. 2007. Structure, Function, and Transport of Lipoproteins in , p 67-79. In Ehrmann M (ed), The Periplasm. ASM Press, Washington, DC. doi: 10.1128/9781555815806.ch4

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Two-Component Signal Transduction Systems
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Figures

Image of FIGURE 1
FIGURE 1

Biogenesis of lipoproteins. Lipoprotein precursors have a consensus sequence, -L-(A/S)-(G/A)-C-, called a lipobox (broken squares), around a signal cleavage site. X represents a residue other than Asp. Lgt, phosphatidylglycerol:prolipoprotein diacylglyceryl-transferase; LspA, prolipoprotein signal peptidase (also called Spase II); Lnt, phospholipid: apolipoprotein transacylase. A Lol pathway discussed later mediates the outer membrane localization of lipoproteins in a manner dependent on sorting signals.

Citation: Tokuda H, Matsuyama S, Tanaka-Masuda K. 2007. Structure, Function, and Transport of Lipoproteins in , p 67-79. In Ehrmann M (ed), The Periplasm. ASM Press, Washington, DC. doi: 10.1128/9781555815806.ch4
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Image of FIGURE 2
FIGURE 2

Sorting and outer membrane localization of lipoproteins through the Lol pathway. “In” and “Out” represent inner membrane-specific and outer membrane-specific lipoproteins, respectively. An ABC transporter, LolCDE, releases outer membrane-specific lipoproteins from the inner membrane, causing the formation of a complex between the released lipoproteins and the periplasmic molecular chaperone LolA. When this complex interacts with outer membrane receptor LolB, the lipoproteins are transferred from LolA to LolB and then localized to the outer membrane. The inner membrane retention signal Asp at position 2 inhibits the recognition of lipoproteins by LolCDE, thereby causing their retention in the inner membrane. Phosphatidylethanolamine plays an important role in the Lol avoidance function of Asp at position 2.

Citation: Tokuda H, Matsuyama S, Tanaka-Masuda K. 2007. Structure, Function, and Transport of Lipoproteins in , p 67-79. In Ehrmann M (ed), The Periplasm. ASM Press, Washington, DC. doi: 10.1128/9781555815806.ch4
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Tables

Generic image for table
TABLE 1

Biochemically confirmed lipoproteins in

Citation: Tokuda H, Matsuyama S, Tanaka-Masuda K. 2007. Structure, Function, and Transport of Lipoproteins in , p 67-79. In Ehrmann M (ed), The Periplasm. ASM Press, Washington, DC. doi: 10.1128/9781555815806.ch4

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