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Mutational analysis of human RNA polymerase II subunit 5 (RPB5): The residues critical for interactions with TFIIF subunit RAP30 and hepatitis B virus X protein
https://doi.org/10.24517/00027528
https://doi.org/10.24517/000275282682b6fa-5bc2-4c0f-8778-911d1bdfc007
| 名前 / ファイル | ライセンス | アクション |
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CA-PR-MURAKAMI-S-215.pdf (672.2 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||
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| 公開日 | 2017-10-05 | |||||||||
| タイトル | ||||||||||
| タイトル | Mutational analysis of human RNA polymerase II subunit 5 (RPB5): The residues critical for interactions with TFIIF subunit RAP30 and hepatitis B virus X protein | |||||||||
| 言語 | ||||||||||
| 言語 | eng | |||||||||
| 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 | journal article | |||||||||
| ID登録 | ||||||||||
| ID登録 | 10.24517/00027528 | |||||||||
| ID登録タイプ | JaLC | |||||||||
| 著者 |
Le, Thi Thu Thuy
× Le, Thi Thu Thuy× Zhang, Shijun× Hayashi, Naoyuki× Yasukawa, Mami× Delgermaa, Luvsanjav× Murakami, Seishi |
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| 著者別表示 |
林, 直之
× 林, 直之
× 村上, 清史
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| 提供者所属 | ||||||||||
| 内容記述タイプ | Other | |||||||||
| 内容記述 | 金沢大学がん研究所 | |||||||||
| 書誌情報 |
Journal of Biochemistry 巻 138, 号 3, p. 215-224, 発行日 2005-09-01 |
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| ISSN | ||||||||||
| 収録物識別子タイプ | ISSN | |||||||||
| 収録物識別子 | 0021-924X | |||||||||
| NCID | ||||||||||
| 収録物識別子タイプ | NCID | |||||||||
| 収録物識別子 | AA00694073 | |||||||||
| DOI | ||||||||||
| 関連タイプ | isIdenticalTo | |||||||||
| 識別子タイプ | DOI | |||||||||
| 関連識別子 | https://doi.org/10.1093/jb/mvi119 | |||||||||
| 出版者 | ||||||||||
| 出版者 | 日本生化学会 = Japanese Biochemical Society | |||||||||
| 抄録 | ||||||||||
| 内容記述タイプ | Abstract | |||||||||
| 内容記述 | RNA polymerase II (RNAPII) subunit 5 (RPB5) is positioned close to DNA downstream of the initiation site and is the site of interaction with several regulators. Hepatitis B virus X protein (HBx) binds the central part of RPB5 to modulate activated transcription, and TFIIF subunit RAP30 interacts with the same part of RPB5 that is critical for the association between TFIIF and RNAPII. However the residues necessary for these interactions remain unknown. Here we report systematic mutagenesis of the central part of RPB5 using two-step alanine scanning libraries to pinpoint critical residues for its binding to RAP30 in the TFIIF complex and/or to HBx, and identified these residues in both mammalian cells and in an in vitro binding assay. Four residues, F76, I104, T111 and S113, are critical for both TFIIF- and HBx-binding, indicating the overlapping nature of the sites of interaction. In addition, V74 and N98 are required for HBx-binding, and T56 and L58 are needed for RAP30-binding. Interestingly the residues exposed to solvent, T111 and S113, are very close to the DNA, implying that two factors may modulate the interaction between DNA and RPB5. © 2005 The Japanese Biochemical Society. | |||||||||
| 権利 | ||||||||||
| 権利情報 | © 2007 The Japanese Biochemical Society. | |||||||||
| 著者版フラグ | ||||||||||
| 出版タイプ | VoR | |||||||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||||||
| 関連URI | ||||||||||
| 識別子タイプ | URI | |||||||||
| 関連識別子 | http://jb.oxfordjournals.org/cgi/content/abstract/138/3/215 | |||||||||
