Opening and Closing of the Hydrophobic Cavity of LolA Coupled to Lipoprotein Binding and Release

Oguchi, Yusuke; Takeda, Kazuki; Watanabe, Shôji; Yokota, Naoko; Miki, Kunio; Tokuda, Harukuni

doi:10.1074/jbc.m804736200

Cited by 34 publications

(45 citation statements)

References 22 publications

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“…It was recently shown that the hydrophobic cavity of LolA opens and closes upon the binding and release of lipoproteins, respectively (8). Moreover, LolA complexed with the outer membrane lipoprotein Pal was found to be accumulated in the periplasm when they were co-overexpressed from an efficient plasmid (16).…”

Section: Resultsmentioning

confidence: 99%

“…1 A, yellow oval). Crystallographic studies involving a LolA(R43L) derivative recently revealed the entrance of the hydrophobic cavity, which was open in this mutant (8). In contrast, the hydrophobic cavity of wild-type LolA was found to open upon lipoprotein binding (8).…”

Section: Resultsmentioning

confidence: 99%

“…The crystal structures of free LolA, mLolB (7), and LolA(R43L) (8) together with the results of biochemical analyses (8, 9, 21) strongly suggest that LolA and LolB accommodate the acyl chains of lipoproteins in their hydrophobic cavities. Furthermore, the hydrophobic cavity of LolA was found to undergo opening and closing upon the binding and release of lipoproteins (8).…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, the hydrophobic cavity of LolA was found to undergo opening and closing upon the binding and release of lipoproteins (8). It was then speculated that the hydrophobic cavity and its conformational change are critically important for the rapid and one-way transfer of lipoproteins from the inner to the outer membrane.…”

Section: Discussionmentioning

confidence: 99%

“…The barrel and the loops, containing 3 ␣-helices, form a hydrophobic cavity. The hydrophobic cavity of LolA, and probably that of LolB too, was recently found to undergo opening and closing upon the binding and release of lipoproteins, respectively (8). The strength of the hydrophobic interaction with lipoproteins was found to be critically important for efficient one-way transfer of lipoproteins from LolA to LolB (9).…”

mentioning

confidence: 99%

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Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB

Okuda

Tokuda

2009

Proc. Natl. Acad. Sci. U.S.A.

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107

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Outer membrane-specific lipoproteins in Escherichia coli are released from the inner membrane by an ATP-binding cassette transporter, the LolCDE complex, which causes the formation of a soluble complex with a periplasmic molecular chaperone, LolA. LolA then transports lipoproteins to the outer membrane where an outer membrane receptor, LolB, incorporates lipoproteins into the outer membrane. The molecular mechanisms underlying the Loldependent lipoprotein sorting have been clarified in detail. However, it remained unclear how Lol factors interact with each other to conduct very efficient lipoprotein transfer in the periplasm where ATP is not available. To address this issue, a photo-reactive phenylalanine analogue, p-benzoyl-phenylalanine, was introduced at various positions of LolA and LolB, of which the overall structures are very similar and comprise an incomplete ␤-barrel with a hydrophobic cavity inside. Cells expressing LolA or LolB derivatives containing the above analogue were irradiated with UV for in vivo photo-cross-linking. These analyses revealed a hot area in the same region of LolA and LolB, through which LolA and LolB interact with each other. This area is located at the entrance of the hydrophobic cavity. Moreover, this area in LolA is involved in the interaction with a membrane subunit, LolC, whereas no cross-linking occurs between LolA and the other membrane subunit, LolE, or ATP-binding subunit LolD, despite the structural similarity between LolC and LolE. The hydrophobic cavities of LolA and LolB were both found to bind lipoproteins inside. These results indicate that the transfer of lipoproteins through Lol proteins occurs in a mouth-to-mouth manner.E. coli ͉ Lol proteins ͉ molecular chaperone ͉ photo-cross-link

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB

Okuda

Tokuda

2009

Proc. Natl. Acad. Sci. U.S.A.

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107

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Lipoprotein Transport: Greasing the Machines of Outer Membrane Biogenesis

Grabowicz

2018

BioEssays

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The Gram-negative outer membrane (OM) is a potent permeability barrier against antibiotics, limiting clinical options amid mounting rates of resistance. The Lol transport pathway delivers lipoproteins to the OM. All the OM assembly machines require one or more OM lipoprotein to function, making the Lol pathway central for all aspects of OM biogenesis. The Lol pathways of many medically important species clearly deviate from the Escherichia coli paradigm, perhaps with implications for efforts to develop novel antibiotics. Moreover, recent work reveals the existence of an undiscovered alternate route for bringing lipoproteins to the OM. Here, lipoprotein transport mechanisms, and the quality control systems that underpin them, is re-examined in context of their diversity.

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The Journey of Lipoproteins Through the Cell

Szewczyk

Collet

2016

Advances in Microbial Physiology

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Opening and Closing of the Hydrophobic Cavity of LolA Coupled to Lipoprotein Binding and Release

Cited by 34 publications

References 22 publications

Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB

Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB

Lipoprotein Transport: Greasing the Machines of Outer Membrane Biogenesis

The Journey of Lipoproteins Through the Cell

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