Item type |
文献 / Documents(1) |
公開日 |
2024-07-11 |
アクセス権 |
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アクセス権 |
open access |
資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
出版社版DOI |
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識別子タイプ |
DOI |
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関連識別子 |
https://doi.org/10.1128/spectrum.00168-23 |
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言語 |
ja |
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関連名称 |
10.1128/spectrum.00168-23 |
出版タイプ |
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出版タイプ |
VoR |
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出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
タイトル |
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タイトル |
Plasmodium Parasite Malate-Quinone Oxidoreductase Functionally Complements a Yeast Deletion Mutant of Mitochondrial Malate Dehydrogenase |
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言語 |
en |
タイトル別表記 |
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その他のタイトル |
Plasmodium MQO Functions in Place of Mitochondrial MDH |
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言語 |
en |
著者 |
伊藤, 剛
カジタ, サヤカ
フジイ, ミノリ
篠原, 康雄
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抄録 |
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内容記述タイプ |
Abstract |
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内容記述 |
The emergence of drug-resistant variants of malaria-causing Plasmodium parasites is a life-threatening problem worldwide. Investigation of the physiological function of individual parasite proteins is a prerequisite for a deeper understanding of the metabolic pathways required for parasite survival and therefore a requirement for the development of novel antimalarials. A Plasmodium membrane protein, malate-quinone oxidoreductase (MQO), is thought to contribute to the tricarboxylic acid (TCA) cycle and the electron transport chain (ETC) and is an antimalarial drug target. However, there is little information on its expression and function. Here, we investigated the function of Plasmodium falciparum MQO (PfMQO) in mitochondria using a yeast heterologous expression system. Using a yeast deletion mutant of mitochondrial malate dehydrogenase (MDH1), which is expected to be functionally similar to MQO, as a background strain, we successfully constructed PfMQO-expressing yeast. We confirmed that expression of PfMQO complemented the growth defect of the MDH1 deletion, indicating that PfMQO can adopt the metabolic role of MDH1 in energy transduction for growth in the recombinant yeast. Analysis of cell fractions confirmed that PfMQO was expressed and enriched in yeast mitochondria. By measuring MQO activity, we also confirmed that PfMQO expressed in yeast mitochondria was active. Measurement of oxygen consumption rates showed that mitochondrial respiration was driven by the TCA cycle through PfMQO. In addition, we found that MQO activity was enhanced when intact mitochondria were sonicated, indicating that the malate binding site of PfMQO is located facing the mitochondrial matrix. |
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言語 |
en |
キーワード |
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言語 |
en |
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主題Scheme |
Other |
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主題 |
MQO |
キーワード |
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言語 |
en |
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主題Scheme |
Other |
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主題 |
Plasmodium |
キーワード |
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言語 |
en |
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主題Scheme |
Other |
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主題 |
energy metabolism |
キーワード |
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言語 |
en |
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主題Scheme |
Other |
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主題 |
heterologous gene expression |
キーワード |
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言語 |
en |
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主題Scheme |
Other |
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主題 |
mitochondria |
キーワード |
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言語 |
en |
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主題Scheme |
Other |
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主題 |
yeast |
書誌情報 |
en : Microbiology Spectrum
巻 11,
号 3,
p. e00168-23,
発行日 2023-04-10
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収録物ID |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
21650497 |
収録物ID |
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収録物識別子タイプ |
NCID |
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収録物識別子 |
AA12883845 |
出版者 |
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出版者 |
American Society for Microbiology |
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言語 |
en |
権利情報 |
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言語 |
en |
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権利情報 |
This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license. |
EID |
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識別子 |
397395 |
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識別子タイプ |
URI |
言語 |
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言語 |
eng |