A Nonconserved Surface of the TFIIB Zinc Ribbon Domain Plays a Direct Role in RNA Polymerase II Recruitment
Author:
Affiliation:
1. Graduate Program in Genetics, State University of New York at Stony Brook, Stony Brook, New York 11794
2. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724
Abstract
Publisher
American Society for Microbiology
Subject
Cell Biology,Molecular Biology
Link
https://journals.asm.org/doi/pdf/10.1128/MCB.24.7.2863-2874.2004
Reference61 articles.
1. Aso, T., J. W. Conaway, and R. C. Conaway. 1994. Role of core promoter structure in assembly of the RNA polymerase II preinitiation complex. J. Biol. Chem. 269 : 26575-26583.
2. Bagby, S., S. Kim, E. Maldonado, K. I. Tong, D. Reinberg, and M. Ikura. 1995. Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein. Cell 82 : 857-867.
3. Mutational analysis of the D1/E1 core helices and the conserved N-terminal region of yeast transcription factor IIB (TFIIB): identification of an N-terminal mutant that stabilizes TATA-binding protein-TFIIB-DNA complexes
4. Barberis, A., C. W. Muller, S. C. Harrison, and M. Ptashne. 1993. Delineation of two functional regions of transcription factor TFIIB. Proc. Natl. Acad. Sci. USA 90 : 5628-5632.
5. Bell, S. D., C. P. Magill, and S. P. Jackson. 2001. Basal and regulated transcription in Archea. Biochem. Soc. Trans. 29 : 392-395.
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