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  1. Public
  2. 研究紀要
  3. 工学部研究報告
  4. 42(2008)
  1. Private
  2. 研究紀要
  3. 工学部研究報告Research reports of the Faculty of Engineering, Kinki University
  4. 42(2008)

Amino acid sequence diversities in TBP, TATA binding protein, of extremely halophilic archaeon Haloarcula japonica strain TR-1

https://kindai.repo.nii.ac.jp/records/7281
https://kindai.repo.nii.ac.jp/records/7281
4a255400-fa02-491f-9f0f-2f66f90e079e
名前 / ファイル ライセンス アクション
AN00063799-20081220-0017.pdf AN00063799-20081220-0017.pdf (903.6 kB)
Item type ☆紀要論文 / Departmental Bulletin Paper(1)
公開日 2010-07-02
タイトル
タイトル Amino acid sequence diversities in TBP, TATA binding protein, of extremely halophilic archaeon Haloarcula japonica strain TR-1
著者 Matsumi, Hironari

× Matsumi, Hironari

Matsumi, Hironari

ja-Kana マツミ, ヒロナリ

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Nakasone, Kaoru

× Nakasone, Kaoru

Nakasone, Kaoru

ja-Kana ナカソネ, カオル

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言語
言語 eng
キーワード
主題 Haloarcula japonica, TATA-box binding protein, TBP, overexpression
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ departmental bulletin paper
著者(英)
言語 en
値 松味, 弘也
著者(英)
言語 en
値 仲宗根, 薫
著者 所属
値 近畿大学大学院システム工学研究科
著者 所属
値 近畿大学大学院システム工学研究科
著者所属(翻訳)
値 Graduate School of Systems Engineering, Kinki University
著者所属(翻訳)
値 Graduate School of Systems Engineering, Kinki University
版
出版タイプ NA
出版タイプResource http://purl.org/coar/version/c_be7fb7dd8ff6fe43
出版者 名前
出版者 近畿大学工学部
書誌情報 近畿大学工学部研究報告
en : Research reports of the School of Engineering, Kinki University

号 42, p. 17-20, 発行日 2008-12-01
ISSN
収録物識別子タイプ ISSN
収録物識別子 0386491X
抄録
内容記述タイプ Abstract
内容記述 The TATA-box binding protein (TBP) is a basal transcription factor involved in transcription initiation in Eukarya and Archaea. Through exhaustive analyses of the whole geneme of extremely halophilic archaeon, Haloarcula japonica strain TR-1, six TBP genes were found and structurally analyzed. These TBPs were designated as TBP1, TBP2, TBP3, TBP4, TBP5 and TBP6, respectively and these TBPs were diverged from other archaeal TBPs that have been known. TBP1 gene was found to encode a polypeptide consisting of 182 amino acid residues, showing 35.0% identity to that of H. marismortui. TBP2 gene was found to encode a polypeptide consisting of 182 amino acid residues, showing 36.5% identity to that of H. marismortui. TBP3 gene was found to encode a polypeptide consisting of 186 amino acid residues, showing 100% identity to that of H. marismortui. TBP4 gene was found to encode a polypeptide consisting of 185 amino acid residues, showing 42.9% identity to that of H. marismortui. TBP5 gene was found to encode a polypeptide consisting of 182 amino acid residues, showing 35.4% identity to that of H. marismortui. TBP6 gene was found to encode a polypeptide consisting of 182 amino acid residues, showing 46.1% identity to that of H. marismortui. By phylogenetic analyses of these six proteins, TBP3 is conserved in amino acid sequence with other archaeal strains including methanogens and thermophiles, It may suggest that the TBP3 is core TBP function in transcriptional initiation such as housekeeping genes. Six histidine-tagged version of the H. japonica TBPs were produced in Escherichia coli in a denature conditions after construction of overexpression plasmids and purified by means of Ni-chelating chromatography.
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内容記述 application/pdf
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