4BRW

Crystal structure of the yeast Dhh1-Pat1 complex

Summary for 4BRW

• Entry DOI: 10.2210/pdb4brw/pdb
• Related: 4BRU
• Descriptor: ATP-DEPENDENT RNA HELICASE DHH1, DNA TOPOISOMERASE 2-ASSOCIATED PROTEIN PAT1, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total)
• Functional Keywords: hydrolase, translational repression, mrnp remodeling, p- bod
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Cytoplasm, P-body: P39517; Cytoplasm: P25644
• Total number of polymer chains: 2
• Total formula weight: 51109.09

Authors

Sharif, H.,Ozgur, S.,Sharma, K.,Basquin, C.,Urlaub, H.,Conti, E. (deposition date: 2013-06-05, release date: 2013-07-24, Last modification date: 2023-12-20)

Primary citation

Sharif, H.,Ozgur, S.,Sharma, K.,Basquin, C.,Urlaub, H.,Conti, E.
Structural Analysis of the Yeast Dhh1-Pat1 Complex Reveals How Dhh1 Engages Pat1, Edc3 and RNA in Mutually Exclusive Interactions
Nucleic Acids Res., 41:8377-, 2013

PubMed Abstract: Translational repression and deadenylation of eukaryotic mRNAs result either in the sequestration of the transcripts in a nontranslatable pool or in their degradation. Removal of the 5' cap structure is a crucial step that commits deadenylated mRNAs to 5'-to-3' degradation. Pat1, Edc3 and the DEAD-box protein Dhh1 are evolutionary conserved factors known to participate in both translational repression and decapping, but their interplay is currently unclear. We report the 2.8 Å resolution structure of yeast Dhh1 bound to the N-terminal domain of Pat1. The structure shows how Pat1 wraps around the C-terminal RecA domain of Dhh1, docking onto the Phe-Asp-Phe (FDF) binding site. The FDF-binding site of Dhh1 also recognizes Edc3, revealing why the binding of Pat1 and Edc3 on Dhh1 are mutually exclusive events. Using co-immunoprecipitation assays and structure-based mutants, we demonstrate that the mode of Dhh1-Pat1 recognition is conserved in humans. Pat1 and Edc3 also interfere and compete with the RNA-binding properties of Dhh1. Mapping the RNA-binding sites on Dhh1 with a crosslinking-mass spectrometry approach shows a large RNA-binding surface around the C-terminal RecA domain, including the FDF-binding pocket. The results suggest a model for how Dhh1-containing messenger ribonucleoprotein particles might be remodeled upon Pat1 and Edc3 binding.

PubMed: 23851565
DOI: 10.1093/NAR/GKT600

Experimental method

X-RAY DIFFRACTION (2.795 Å)