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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
著者: Le, Thi Thu Thuy
Zhang, Shijun
Hayashi, Naoyuki link image
Yasukawa, Mami
Delgermaa, Luvsanjav
Murakami, Seishi link image
林, 直之
村上, 清史
発行日: 2005年 9月
出版社(者): 日本生化学会 = Japanese Biochemical Society
雑誌名: Journal of Biochemistry
ISSN: 0021-924X
巻: 138
号: 3
開始ページ: 215
終了ページ: 224
キーワード: Alanine scanning
Coactivation
HBx
RAP30
RPB5
TFIIF
抄録: 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.
URI: http://hdl.handle.net/2297/14550
関連URI: http://jb.oxfordjournals.org/cgi/content/abstract/138/3/215
資料種別: Journal Article
権利関係: © 2007 The Japanese Biochemical Society.
版表示: publisher
出現コレクション:1. 査読済論文

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