ArticleThe Journal of biological chemistry2014
DNA binding by Sgf11 protein affects histone H2B deubiquitination by Spt-Ada-Gcn5-acetyltransferase (SAGA).
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Zinc Metalloproteins in Epigenetics and Their Crosstalk.Life (Basel, Switzerland) · 2021Review
- The SAGA continues: The rise of cis- and trans-histone crosstalk pathways.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- Dynamic modules of the coactivator SAGA in eukaryotic transcription.Experimental & molecular medicine · 2020Review
- The histone H4 basic patch regulates SAGA-mediated H2B deubiquitination and histone acetylation.The Journal of biological chemistry · 2020Article
- Deubiquitination in prostate cancer progression: role of USP22.Journal of cancer metastasis and treatment · 2020Article
- Distinct requirements of linker DNA and transcriptional activators in promoting SAGA-mediated nucleosome acetylation.The Journal of biological chemistry · 2018Article
- Enzymatic modules of the SAGA chromatin-modifying complex play distinct roles inGenes & development · 2017Article
- Structural Basis of Eco1-Mediated Cohesin Acetylation.Scientific reports · 2017Article
- Cytoplasmic ATXN7L3B Interferes with Nuclear Functions of the SAGA Deubiquitinase Module.Molecular and cellular biology · 2016Article
- Review
- ATXN7L3 and ENY2 Coordinate Activity of Multiple H2B Deubiquitinases Important for Cellular Proliferation and Tumor Growth.Molecular cell · 2016Article
- Structural basis for histone H2B deubiquitination by the SAGA DUB module.Science (New York, N.Y.) · 2016Article
- SAGA and SAGA-like SLIK transcriptional coactivators are structurally and biochemically equivalent.The Journal of biological chemistryArticle
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The yeast Spt-Ada-Gcn5-acetyltransferase (SAGA) complex is a transcription coactivator that contains a histone H2B deubiquitination activity mediated by its Ubp8 subunit. Full enzymatic activity requires the formation of a quaternary complex, the deubiquitination module (DUBm) of SAGA, which is composed of Ubp8, Sus1, Sgf11, and Sgf73. The crystal structures of the DUBm have shed light on the structure/function relationship of this complex. Specifically, both Sgf11 and Sgf73 contain zinc finger domains (ZnF) that appear essential for the DUBm activity. Whereas Sgf73 N-terminal ZnF is important for DUBm stability, Sgf11 C-terminal ZnF appears to be involved in DUBm function. To further characterize the role of these two zinc fingers, we have solved their structure by NMR. We show that, contrary to the previously reported structures, Sgf73 ZnF adopts a C2H2 coordination with unusual tautomeric forms for the coordinating histidines. We further report that the Sgf11 ZnF, but not the Sgf73 ZnF, binds to nucleosomal DNA with a binding interface composed of arginine residues located within the ZnF α-helix. Mutational analyses both in vitro and in vivo provide evidence for the functional relevance of our structural observations. The combined interpretation of our results leads to an uncommon ZnF-DNA interaction between the SAGA DUBm and nucleosomes, thus providing further functional insights into SAGA's epigenetic modulation of the chromatin structure.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.