Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins-Reference-Cited by-同舟云学术

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Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins

Published:2011-11-20 Issue:12 Volume:18 Page:1414-1420
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Tripsianes Konstantinos,Madl Tobias,Machyna Martin,Fessas Dimitrios,Englbrecht Clemens,Fischer Utz,Neugebauer Karla M,Sattler Michael

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.2185.pdf

Reference57 articles.

1. Bedford, M.T. & Clarke, S.G. Protein arginine methylation in mammals: who, what, and why. Mol. Cell 33, 1–13 (2009).

2. Siomi, M.C., Mannen, T. & Siomi, H. How does the royal family of Tudor rule the PIWI-interacting RNA pathway? Genes Dev. 24, 636–646 (2010).

3. Boisvert, F.M., Cote, J., Boulanger, M.C. & Richard, S. A proteomic analysis of arginine-methylated protein complexes. Mol. Cell. Proteomics 2, 1319–1330 (2003).

4. Brahms, H., Meheus, L., de Brabandere, V., Fischer, U. & Luhrmann, R. Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA 7, 1531–1542 (2001).

5. Friesen, W.J., Massenet, S., Paushkin, S., Wyce, A. & Dreyfuss, G. SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. Mol. Cell 7, 1111–1117 (2001).

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