SAGA-associated factor

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**[[3me9]], [[3mea]], [[3met]], [[3meu]], [[3mev]], [[3mew]], [[3mp1]], [[3mp6]], [[5c0m]] – hSGF tudor domain + histone H3 peptide – human<br />
**[[3me9]], [[3mea]], [[3met]], [[3meu]], [[3mev]], [[3mew]], [[3mp1]], [[3mp6]], [[5c0m]] – hSGF tudor domain + histone H3 peptide – human<br />
**[[3lx7]], [[3mp8]] - hSGF tudor domain <br />
**[[3lx7]], [[3mp8]] - hSGF tudor domain <br />
 +
**[[5c0m]] - hSGF tudor domain + CABRA containing peptide <br />
*SGF73
*SGF73

Revision as of 20:54, 2 October 2017

Structure of SGF11 (pink) in the SAGA complex with Sus1 (green) , SGF73 (magenta), ubiquitin (yellow), UB8P (grey), glycerol and Zn+2 ions (grey) (PDB entry 3mhs)

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3D structures of SAGA-associated factor

Updated on 02-October-2017

References

  1. ↑ Mischerikow N, Spedale G, Altelaar AF, Timmers HT, Pijnappel WW, Heck AJ. In-depth profiling of post-translational modifications on the related transcription factor complexes TFIID and SAGA. J Proteome Res. 2009 Nov;8(11):5020-30. doi: 10.1021/pr900449e. PMID:19731963 doi:http://dx.doi.org/10.1021/pr900449e
  2. ↑ Schram AW, Baas R, Jansen PW, Riss A, Tora L, Vermeulen M, Timmers HT. A dual role for SAGA-associated factor 29 (SGF29) in ER stress survival by coordination of both histone H3 acetylation and histone H3 lysine-4 trimethylation. PLoS One. 2013 Jul 23;8(7):e70035. doi: 10.1371/journal.pone.0070035. Print 2013. PMID:23894581 doi:http://dx.doi.org/10.1371/journal.pone.0070035
  3. ↑ Deng X, Zhou H, Zhang G, Wang W, Mao L, Zhou X, Yu Y, Lu H. Sgf73, a subunit of SAGA complex, is required for the assembly of RITS complex in fission yeast. Sci Rep. 2015 Oct 7;5:14707. doi: 10.1038/srep14707. PMID:26443059 doi:http://dx.doi.org/10.1038/srep14707

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman

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