ArticleNucleic acids research2014
Crystal structure, mutational analysis and RNA-dependent ATPase activity of the yeast DEAD-box pre-mRNA splicing factor Prp28.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- SRSF1 interactome determined by proximity labeling reveals direct interaction with spliceosomal RNA helicase DDX23.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A distinct assembly pathway of the human 39S late pre-mitoribosome.Nature communications · 2021Article
- Activation of Prp28 ATPase by phosphorylated Npl3 at a critical step of spliceosome remodeling.Nature communications · 2021Article
- Mechanism of 5' splice site transfer for human spliceosome activation.Science (New York, N.Y.) · 2019Article
- Domain Requirements and Genetic Interactions of the Mud1 Subunit of theG3 (Bethesda, Md.) · 2019Article
- SMA1, a homolog of the splicing factor Prp28, has a multifaceted role in miRNA biogenesis in Arabidopsis.Nucleic acids research · 2018Article
- Article
- Understanding pre-mRNA splicing through crystallography.Methods (San Diego, Calif.) · 2017Review
- Structure-function analysis and genetic interactions of the Luc7 subunit of the Saccharomyces cerevisiae U1 snRNP.RNA (New York, N.Y.) · 2016Article
- A spliceosome intermediate with loosely associated tri-snRNP accumulates in the absence of Prp28 ATPase activity.Nature communications · 2016Article
- Structural analysis of the spliceosomal RNA helicase Prp28 from the thermophilic eukaryote Chaetomium thermophilum.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Autoinhibitory Interdomain Interactions and Subfamily-specific Extensions Redefine the Catalytic Core of the Human DEAD-box Protein DDX3.The Journal of biological chemistry · 2016Article
- Structure-function analysis and genetic interactions of the Yhc1, SmD3, SmB, and Snp1 subunits of yeast U1 snRNP and genetic interactions of SmD3 with U2 snRNP subunit Lea1.RNA (New York, N.Y.) · 2015Article
- Synergistic effects of ATP and RNA binding to human DEAD-box protein DDX1.Nucleic acids research · 2015Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Yeast Prp28 is a DEAD-box pre-mRNA splicing factor implicated in displacing U1 snRNP from the 5' splice site. Here we report that the 588-aa Prp28 protein consists of a trypsin-sensitive 126-aa N-terminal segment (of which aa 1-89 are dispensable for Prp28 function in vivo) fused to a trypsin-resistant C-terminal catalytic domain. Purified recombinant Prp28 and Prp28-(127-588) have an intrinsic RNA-dependent ATPase activity, albeit with a low turnover number. The crystal structure of Prp28-(127-588) comprises two RecA-like domains splayed widely apart. AMPPNP•Mg2+ is engaged by the proximal domain, with proper and specific contacts from Phe194 and Gln201 (Q motif) to the adenine nucleobase. The triphosphate moiety of AMPPNP•Mg2+ is not poised for catalysis in the open domain conformation. Guided by the Prp28•AMPPNP structure, and that of the Drosophila Vasa•AMPPNP•Mg2+•RNA complex, we targeted 20 positions in Prp28 for alanine scanning. ATP-site components Asp341 and Glu342 (motif II) and Arg527 and Arg530 (motif VI) and RNA-site constituent Arg476 (motif Va) are essential for Prp28 activity in vivo. Synthetic lethality of double-alanine mutations highlighted functionally redundant contacts in the ATP-binding (Phe194-Gln201, Gln201-Asp502) and RNA-binding (Arg264-Arg320) sites. Overexpression of defective ATP-site mutants, but not defective RNA-site mutants, elicited severe dominant-negative growth defects.
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