Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Structural insights into the assembly and function of the SAGA deubiquitinating module.

Science (New York, N.Y.) | May 21, 2010

SAGA is a transcriptional coactivator complex that is conserved across eukaryotes and performs multiple functions during transcriptional activation and elongation. One role is deubiquitination of histone H2B, and this activity resides in a distinct subcomplex called the deubiquitinating module (DUBm), which contains the ubiquitin-specific protease Ubp8, bound to Sgf11, Sus1, and Sgf73. The deubiquitinating activity depends on the presence of all four DUBm proteins. We report here the 1.90 angstrom resolution crystal structure of the DUBm bound to ubiquitin aldehyde, as well as the 2.45 angstrom resolution structure of the uncomplexed DUBm. The structure reveals an arrangement of protein domains that gives rise to a highly interconnected complex, which is stabilized by eight structural zinc atoms that are critical for enzymatic activity. The structure suggests a model for how interactions with the other DUBm proteins activate Ubp8 and allows us to speculate about how the DUBm binds to monoubiquitinated histone H2B in nucleosomes.

Pubmed ID: 20395473 RIS Download

Mesh terms: Aldehydes | Crystallography, X-Ray | Endopeptidases | Histone Acetyltransferases | Histones | Models, Biological | Models, Molecular | Nuclear Proteins | Nucleosomes | Protein Binding | Protein Conformation | Protein Structure, Tertiary | RNA-Binding Proteins | Saccharomyces cerevisiae Proteins | Trans-Activators | Transcription Factors | Ubiquitin | Ubiquitinated Proteins | Ubiquitination | Ubiquitins | Zinc | Zinc Fingers

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

  • Agency: NIGMS NIH HHS, Id: Y1-GM-1104
  • Agency: NIGMS NIH HHS, Id: R01 GM095822
  • Agency: NIGMS NIH HHS, Id: F32 GM089037
  • Agency: NIGMS NIH HHS, Id: F32GM089037
  • Agency: Howard Hughes Medical Institute, Id: Y1-CO-1020
  • Agency: NCI NIH HHS, Id:

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

We have not found any resources mentioned in this publication.