SAGA-associated factor

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(New page: <StructureSection load='3mhs' size='350' side='right' caption='Structure of SGF11 in the SAGA complex with Sus1, SGF73 and UB8P (PDB entry 3mhs)' scene=''> '''SAGA-associated fact...)
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<StructureSection load='3mhs' size='340' side='right' caption='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]])' scene=''>
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<StructureSection load='3mhs' size='350' side='right' caption='Structure of SGF11 in the SAGA complex with Sus1, SGF73 and UB8P (PDB entry [[3mhs]])' scene=''>
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'''SAGA-associated factor''' (SGF) is part of the coactivator complex SAGA (Spt-Ada-Gcn5-Acetyl transferase) which facilitates transcription of stress-activated genes. SGF29 binds methylated lysine of histone H3 and is involved in transcriptional regulation. SGF11 is required for the deubiuqitination of histone H2B and for the maintenance of steady-state H3 methylation level.
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'''SAGA-associated factor''' (SGF) is part of the coactivator complex SAGA ('''S'''pt-'''A'''da-'''G'''cn5-'''A'''cetyl transferase) which facilitates transcription of stress-activated genes<ref>PMID:19731963</ref>.<br />
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* '''SGF11''' is required for the deubiuqitination of histone H2B and for the maintenance of steady-state H3 methylation level.<br />
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* '''SGF29''' binds methylated lysine of histone H3 and is involved in transcriptional regulation<ref>PMID:23894581</ref>.<br />
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* '''SGF73''' is required for the assembly of RITS complex in yeast<ref>PMID:26443059</ref>.<br />.
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</StructureSection>
==3D structures of SAGA-associated factor==
==3D structures of SAGA-associated factor==
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===SGF11===
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*SGF11
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[[2lo2]] – ySGF zinc finger domain – yeast – NMR<br />
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**[[2lo2]] – ySGF zinc finger domain – yeast – NMR<br />
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[3kik]], [[3kjl]] – ySGF Sus1-binding domain + Sus1 <br />
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**[[3kik]], [[3kjl]] – ySGF Sus1-binding domain + Sus1 <br />
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[[3mhh]], [[3m99]], [[4fip]], [[4fjc]], [[4fk5]] – yUBP8 + Sus1 +SGF73 - yeast<br />
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**[[3mhh]], [[3m99]], [[4fip]], [[4fjc]], [[4fk5]], [[4wa6]] – ySGF11 + SGF73 + yUBP8 + SUS1 <br />
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[[3mhs]] – yUBP8 + Sus1 +SGF73 + ubiquitin<br />
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**[[3mhs]], [[6aqr]] – ySGF11 + SGF73 + yUBP8 + SUS1 + ubiquitin<br />
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**[[4w4u]], [[6aqr]] – ySGF11 + ySGF73 + SUS1 + ubiquitin carboxyl terminal hydrolase<br />
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**[[4zux]] – SGF11 + SGF73 + yUBP8 + SUS1 + ubiquitin + histone H3.2, H4, H2A, H2B + DNA<br />
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**[[6tbm]] – KpSGF + TBP + SPT20 + SPT8 + transcription coactivator HFI1 + TFIID + polyubiquitin + SUS1 + transcription-associated protein – ''Komagataela phaffii'' - Cryo EM<br />
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===SGF29===
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*SGF29
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[[3me9]], [[3mea]], [[3met]], [[3meu]], [[3mev]], [[3mew]], [[3mp1]], [[3mp6]] – hSGF tudor domain + histone H3 peptide – human<br />
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**[[3me9]], [[3mea]], [[3met]], [[3meu]], [[3mev]], [[3mew]], [[3mp1]], [[3mp6]], [[5c0m]] – hSGF tudor domain + histone H3 peptide – human<br />
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[[3lx7]], [[3mp8]] - hSGF tudor domain <br />
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**[[3lx7]], [[3mp8]] - hSGF tudor domain <br />
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**[[5c0m]] - hSGF tudor domain + CABRA containing peptide <br />
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===SGF73===
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*SGF73
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[[2lo3]] – ySGF zinc finger domain – NMR<br />
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**[[6t9i]], [[6t9k]], [[6t9l]] – ySGF in transcription coactivator SAGA – Cryo EM<br />
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**[[2lo3]] – ySGF zinc finger domain – NMR<br />
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**[[3mhh]], [[3m99]], [[4fip]], [[4fjc]], [[4fk5]], [[4wa6]] – ySGF73 + yUBP8 + Sus1 <br />
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**[[3mhs]] – ySGF73 + yUBP8 + Sus1 + ubiquitin<br />
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**[[6tb4]] – KpSGF + TBP + SPT20 + transcription coactivator HFI1 + TFIID + ADA3 + transcription-associated protein - Cryo EM<br />
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}}
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== References ==
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<references/>
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[[Category: Topic Page]]

Current revision

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)

Drag the structure with the mouse to rotate

3D structures of SAGA-associated factor

Updated on 09-March-2022

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

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Michal Harel, Joel L. Sussman

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