Substitution of tryptophan 89 with tyrosine switches the DNA binding mode of PC4-Reference-Cited by-同舟云学术

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Substitution of tryptophan 89 with tyrosine switches the DNA binding mode of PC4

Published:2015-03-05 Issue:1 Volume:5 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Huang Jinguang,Zhao Yanxiang,Liu Huaian,Huang Dan,Cheng Xiankun,Zhao Wensheng,Taylor Ian A.,Liu Junfeng,Peng You-Liang

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep08789.pdf

Reference26 articles.

1. Henry, N. L., Bushnell, D. A. & Kornberg, R. D. A yeast transcriptional stimulatory protein similar to human PC4. J. Biol. Chem. 271, 21842–21847 (1996).

2. Knaus, R., Pollock, R. & Guarente, L. Yeast SUB1 is a suppressor of TFIIB mutations and has homology to the human co-activator PC4. EMBO J. 15, 1933–1940 (1996).

3. Werten, S. et al. High-affinity DNA binding by the C-terminal domain of the transcriptional coactivator PC4 requires simultaneous interaction with two opposing unpaired strands and results in helix destabilization. J. Mol. Biol. 276, 367–377 (1998).

4. Werten, S. et al. Interaction of PC4 with melted DNA inhibits transcription. EMBO J. 17, 5103–5111 (1998).

5. Rosonina, E., Willis, I. M. & Manley, J. L. Sub1 functions in osmoregulation and in transcription by both RNA polymerases II and III. Mol. Cell. Biol. 29, 2308–2321 (2009).

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