Structure-Function Analysis of the Human TFIIB-Related Factor II Protein Reveals an Essential Role for the C-Terminal Domain in RNA Polymerase III Transcription
Author:
Affiliation:
1. Genetics Program, Stony Brook University, Stony Brook, New York 11794
2. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724
3. Howard Hughes Medical Institute, 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.25.21.9406-9418.2005
Reference44 articles.
1. Andrau, J. C., A. Sentenac, and M. Werner. 1999. Mutagenesis of yeast TFIIIB70 reveals C-terminal residues critical for interaction with TBP and C34. J. Mol. Biol. 288 : 511-520.
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. Barberis, A., C. W. Müller, S. C. Harrison, and M. Ptashne. 1993. Delineation of two functional regions of transcription factor TFIIB. Proc. Natl. Acad. Sci. USA 90 : 5628-5632.
4. Buratowski, S., and H. Zhou. 1993. Functional domains of transcription factor TFIIB. Proc. Natl. Acad. Sci. USA 90 : 5633-5637.
5. Bushnell, D. A., K. D. Westover, R. E. Davis, and R. D. Kornberg. 2004. Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Å. Science 303 : 983-988.
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