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  1. B300 農学部/生命農学研究科
  2. B300a 雑誌掲載論文
  3. 学術雑誌

Identification and biochemical characterization of a heteromeric cis-prenyltransferase from the thermophilic archaeon Archaeoglobus fulgidus

http://hdl.handle.net/2237/0002003778
http://hdl.handle.net/2237/0002003778
ed49de2c-aac6-4919-bfbc-f545a13c55ae
名前 / ファイル ライセンス アクション
manuscript_forrepository.pdf manuscript_forrepository.pdf (3.7 MB)
 Download is available from 2023/5/31.
Item type itemtype_ver1(1)
公開日 2022-09-14
タイトル
タイトル Identification and biochemical characterization of a heteromeric cis-prenyltransferase from the thermophilic archaeon Archaeoglobus fulgidus
言語 en
著者 Sompiyachoke, Kitty

× Sompiyachoke, Kitty

en Sompiyachoke, Kitty

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Nagasaka, Arisa

× Nagasaka, Arisa

en Nagasaka, Arisa

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Ito, Tomokazu

× Ito, Tomokazu

en Ito, Tomokazu

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Hemmi, Hisashi

× Hemmi, Hisashi

en Hemmi, Hisashi

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アクセス権
アクセス権 embargoed access
アクセス権URI http://purl.org/coar/access_right/c_f1cf
権利
言語 en
権利情報 This is a pre-copyedited, author-produced version of an article accepted for publication in [The Journal of Biochemistry] following peer review. The version of record [Kitty Sompiyachoke, Arisa Nagasaka, Tomokazu Ito, Hisashi Hemmi, Identification and biochemical characterization of a heteromeric cis-prenyltransferase from the thermophilic archaeon Archaeoglobus fulgidus, The Journal of Biochemistry, Volume 171, Issue 6, June 2022, Pages 641–651, https://doi.org/10.1093/jb/mvac022] is available online at: https://doi.org/10.1093/jb/mvac022.
キーワード
主題Scheme Other
主題 archaea
キーワード
主題Scheme Other
主題 cis-prenyl transferase
キーワード
主題Scheme Other
主題 dolichol
キーワード
主題Scheme Other
主題 enzyme structure
キーワード
主題Scheme Other
主題 isoprenoid
内容記述
内容記述 cis-Prenyltransferases (cPTs) form linear polyprenyl pyrophosphates, the precursors of polyprenyl or dolichyl phosphates that are essential for cell function in all living organisms. Polyprenyl phosphate serves as a sugar carrier for peptidoglycan cell wall synthesis in bacteria, a role that dolichyl phosphate performs analogously for protein glycosylation in eukaryotes and archaea. Bacterial cPTs are characterized by their homodimeric structure, while cPTs from eukaryotes usually require two distantly homologous subunits for enzymatic activity. This study identifies the subunits of heteromeric cPT, Af1219 and Af0707, from a thermophilic sulphur-reducing archaeon, Archaeoglobus fulgidus. Both subunits are indispensable for cPT activity, and their protein–protein interactions were demonstrated by a pulldown assay. Gel filtration chromatography and chemical cross-linking experiments suggest that Af1219 and Af0707 likely form a heterotetramer complex. Although this expected subunit composition agrees with a reported heterotetrameric structure of human hCIT/NgBR cPT complex, the similarity of the quaternary structures is likely a result of convergent evolution.
言語 en
内容記述タイプ Abstract
出版者
言語 en
出版者 Oxford University Press
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
関連情報
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 https://doi.org/10.1093/jb/mvac022
収録物識別子
収録物識別子タイプ PISSN
収録物識別子 0021-924X
書誌情報 en : The Journal of Biochemistry

巻 171, 号 6, p. 641-651, 発行日 2022-06
ファイル公開日
日付 2023-06-01
日付タイプ Available
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