The α subunit C-terminal domain (αCTD) of RNA polymerase (RNAP) is a key element in transcription activation in__Escherichia coli__, possessing determinants responsible for the interaction of RNAP with DNA and with transcription factors. Here, the crystal structure of__E. coli__αCTD (α subunit resid
✦ LIBER ✦
Interaction of the C-terminal domain of the E. coli RNA polymerase α subunit with the UP element: recognizing the backbone structure in the minor groove surface
✍ Scribed by Kazuhiro Yasuno; Toshio Yamazaki; Yoshiyuki Tanaka; Takashi S Kodama; Akimasa Matsugami; Masato Katahira; Akira Ishihama; Yoshimasa Kyogoku
- Book ID
- 115630743
- Publisher
- Elsevier Science
- Year
- 2001
- Tongue
- English
- Weight
- 567 KB
- Volume
- 306
- Category
- Article
- ISSN
- 0022-2836
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Structure of the Escherichia coli RNA po
✍
Lara-González, Samuel ;Birktoft, Jens J. ;Lawson, Catherine L.
📂
Article
📅
2010
🏛
International Union of Crystallography
🌐
English
⚖ 883 KB
Transcription activation at the Escheric
✍
David C. Grainger; Tamara A. Belyaeva; David J. Lee; Eva I. Hyde; Stephen J. W.
📂
Article
📅
2004
🏛
John Wiley and Sons
🌐
English
⚖ 442 KB
Crystal structure of the in vivo-assembl
✍
Valerie Lamour; Lars F. Westblade; Elizabeth A. Campbell; Seth A. Darst
📂
Article
📅
2009
🏛
Elsevier Science
🌐
English
⚖ 408 KB
Interactions of the XylS regulators with
✍
Raquel Ruiz; Juan L Ramos; Susan M Egan
📂
Article
📅
2001
🏛
Elsevier Science
🌐
English
⚖ 456 KB
The C-terminal domains of the RNA polyme
✍
Sarah M McLeod; Sarah E Aiyar; Richard L Gourse; Reid C Johnson
📂
Article
📅
2002
🏛
Elsevier Science
🌐
English
⚖ 707 KB
A novel method for the production of in
✍
Kelly-Anne Twist; Seyyed I. Husnain; Josef D. Franke; Deepti Jain; Elizabeth A.
📂
Article
📅
2011
🏛
Cold Spring Harbor Laboratory Press
🌐
English
⚖ 751 KB
## Abstract The biochemical characterization of the bacterial transcription cycle has been greatly facilitated by the production and characterization of targeted RNA polymerase (RNAP) mutants. Traditionally, RNAP preparations containing mutant subunits have been produced by reconstitution of denatu