Membrane Topology and Functional Importance of the Periplasmic Region of ABC Transporter LolCDE
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- YASUDA Masaki
- Institute of Molecular and Cellular Biosciences, The University of Tokyo
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- IGUCHI-YOKOYAMA Asako
- Institute of Molecular and Cellular Biosciences, The University of Tokyo
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- MATSUYAMA Shin-ichi
- Department of Life Science, Rikkyo University
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- TOKUDA Hajime
- Institute of Molecular and Cellular Biosciences, The University of Tokyo
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- NARITA Shin-ichiro
- Institute of Molecular and Cellular Biosciences, The University of Tokyo
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The LolCDE complex is an ATP-binding cassette transporter that mediates the release of newly synthesized lipoproteins from the cytoplasmic membrane of gram-negative bacteria, which results in the initiation of outer-membrane sorting of lipoproteins through the Lol pathway. LolCDE is composed of one copy each of membrane subunits LolC and LolE, and two copies of nucleotide-binding subunit LolD. In this study, we examined the membrane topology of LolC and LolE by PhoA fusion analysis. Both LolC and LolE were found to have four transmembrane segments with a large periplasmic loop exposed to the periplasm. Despite similarities in sequence and topology, the accessibility of a sulfhydryl reagent to Cys introduced into the periplasmic loop suggested that the structure of the periplasmic region differs between LolC and LolE. Inhibition of the release of lipoproteins by the sulfhydryl reagent supported a previous proposal that LolC and LolE have distinct functions.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 73 (10), 2310-2316, 2009
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681453880192
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- NII論文ID
- 10027547063
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- NII書誌ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 10419479
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- 使用不可