ArticleThe Journal of biological chemistry2010
Structural basis for the interaction between yeast Spt-Ada-Gcn5 acetyltransferase (SAGA) complex components Sgf11 and Sus1.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 38 citations in OpenAlex.
- Peculiarities of theInternational journal of molecular sciences · 2025Article
- The nuclear pore complex acts as a hub for pri-miRNA transcription and processing in plants.Nucleic acids research · 2025Article
- Functional implications of paralog genes in polyglutamine spinocerebellar ataxias.Human genetics · 2023Review
- Potent macrocycle inhibitors of the human SAGA deubiquitinating module.Cell chemical biology · 2022Article
- Molecular Mechanisms of DUBs Regulation in Signaling and Disease.International journal of molecular sciences · 2021Review
- The SAGA chromatin-modifying complex: the sum of its parts is greater than the whole.Genes & development · 2020Review
- An insight into structural plasticity and conformational transitions of transcriptional co-activator Sus1.PloS one · 2020Article
- Sharing the SAGA.Trends in biochemical sciences · 2017Review
- Cytoplasmic ATXN7L3B Interferes with Nuclear Functions of the SAGA Deubiquitinase Module.Molecular and cellular biology · 2016Article
- CTCF and Sgfl1 proteins form alternative complexes with ENY2 proteins.Doklady. Biochemistry and biophysics · 2016Article
- The nucleoporin Mlp2 is involved in chromosomal distribution during mitosis in trypanosomatids.Nucleic acids research · 2015Article
- Highly conserved ENY2/Sus1 protein binds to Drosophila CTCF and is required for barrier activity.Epigenetics · 2014Article
- Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export.Nucleic acids research · 2014Article
- Rapid identification of mRNA processing defects with a novel single-cell yeast reporter.RNA (New York, N.Y.) · 2014Article
- Mechanisms for regulating deubiquitinating enzymes.Protein science : a publication of the Protein Society · 2014Review
- An implementation of hydrophobic force in implicit solvent molecular dynamics simulation for packed proteins.Journal of molecular modeling · 2013Article
- A novel role for Sem1 and TREX-2 in transcription involves their impact on recruitment and H2B deubiquitylation activity of SAGA.Nucleic acids research · 2013Article
- Nuclear pore complex composition: a new regulator of tissue-specific and developmental functions.Nature reviews. Molecular cell biology · 2012Review
- Functional and structural characterization of the mammalian TREX-2 complex that links transcription with nuclear messenger RNA export.Nucleic acids research · 2012Article
- A new chapter in the transcription SAGA.Current opinion in structural biology · 2011Review
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Sus1 is a central component of the yeast gene gating machinery, the process by which actively transcribing genes such as GAL1 become associated with nuclear pore complexes. Sus1 is a component of both the SAGA transcriptional co-activator complex and the TREX-2 complex that binds to nuclear pore complexes. TREX-2 contains two Sus1 chains that have an articulated helical hairpin fold, enabling them to wrap around an extended alpha-helix in Sac3, following a helical hydrophobic stripe. In SAGA, Sus1 binds to Sgf11 and has been proposed to provide a link between SAGA and TREX-2. We present here the crystal structure of the complex between Sus1 and the N-terminal region of Sgf11 that forms an extended alpha-helix around which Sus1 wraps in a manner that shares some similarities with the Sus1-Sac3 interface in TREX-2. However, the Sus1-binding site on Sgf11 is somewhat shorter than on Sac3 and is based on a narrower hydrophobic stripe. Engineered mutants that disrupt the Sgf11-Sus1 interaction in vitro confirm the importance of the hydrophobic helical stripe in molecular recognition. Helix alpha1 of the Sus1-articulated hairpin does not bind directly to Sgf11 and adopts a wide range of conformations within and between crystal forms, consistent with the presence of a flexible hinge and also with results from previous extensive mutagenesis studies (Klöckner, C., Schneider, M., Lutz, S., Jani, D., Kressler, D., Stewart, M., Hurt, E., and Köhler, A. (2009) J. Biol. Chem. 284, 12049-12056). A single Sus1 molecule cannot bind Sgf11 and Sac3 simultaneously and this, combined with the structure of the Sus1-Sgf11 complex, indicates that Sus1 forms separate subcomplexes within SAGA and TREX-2.
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