ArticleNucleic acids research1997
Genetic interactions of conserved regions in the DEAD-box protein Prp28p.
Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 32 citations in OpenAlex.
- The H-subunit of the restriction endonuclease CglI contains a prototype DEAD-Z1 helicase-like motor.Nucleic acids research · 2018Article
- An aromatic-rich loop couples DNA binding and ATP hydrolysis in the PriA DNA helicase.Nucleic acids research · 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
- Crystal structure, mutational analysis and RNA-dependent ATPase activity of the yeast DEAD-box pre-mRNA splicing factor Prp28.Nucleic acids research · 2014Article
- Structural and functional analysis of the human spliceosomal DEAD-box helicase Prp28.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Insight into the roles of helicase motif Ia by characterizing Fanconi anemia group J protein (FANCJ) patient mutations.The Journal of biological chemistry · 2014Article
- Structure-function analysis of the Yhc1 subunit of yeast U1 snRNP and genetic interactions of Yhc1 with Mud2, Nam8, Mud1, Tgs1, U1 snRNA, SmD3 and Prp28.Nucleic acids research · 2014Article
- Structure-function analysis of the 5' end of yeast U1 snRNA highlights genetic interactions with the Msl5*Mud2 branchpoint-binding complex and other spliceosome assembly factors.Nucleic acids research · 2013Article
- The DEAD-box RNA helicase-like Utp25 is an SSU processome component.RNA (New York, N.Y.) · 2010Article
- A conserved phenylalanine of motif IV in superfamily 2 helicases is required for cooperative, ATP-dependent binding of RNA substrates in DEAD-box proteins.Molecular and cellular biology · 2008Article
- Allosteric activation of the ATPase activity of the Escherichia coli RhlB RNA helicase.The Journal of biological chemistry · 2008Article
- Mutation of the arginine finger in the active site of Escherichia coli DbpA abolishes ATPase and helicase activity and confers a dominant slow growth phenotype.Nucleic acids research · 2008Article
- Characterization of the ATPase and unwinding activities of the yeast DEAD-box protein Has1p and the analysis of the roles of the conserved motifs.Nucleic acids research · 2005Article
- Comparative analysis of editosome proteins in trypanosomatids.Nucleic acids research · 2003Article
- Functional conservation of Dhh1p, a cytoplasmic DExD/H-box protein present in large complexes.Nucleic acids research · 2003Article
- Restoration of nucleotide excision repair in a helicase-deficient XPD mutant from intragenic suppression by a trichothiodystrophy mutation.Molecular and cellular biology · 2001Article
- Article
- Characterization and mutational analysis of yeast Dbp8p, a putative RNA helicase involved in ribosome biogenesis.Nucleic acids research · 2001Article
- A new twist on RNA helicases: DExH/D box proteins as RNPases.Nature structural biology · 2001Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The yeast PRP28 g ene has been implicated in nuclear precursor messenger RNA (pre-mRNA) splicing, a two-step reaction involved in a multitude of RNA structural alterations. Prp28p, the gene product of PRP28 , is a member of the evolutionarily conserved DEAD-box proteins (DBPs). Members of DBPs are involved in a variety of RNA-related biochemical processes, presumably by their putative RNA helicase activities. Prp28p has been speculated to play a role in melting the duplex between U4 and U6 small nuclear RNAs (snRNAs), leading to the formation of an active spliceosome. To study the function of Prp28p and its interactions with other components of the splicing machinery, we have isolated and characterized a large number of prp28 conditional mutants. Strikingly, many of these prp28 mutations are localized in the highly conserved motifs found in all the DBPs. Intragenic reversion analysis suggests that regions of motifs II, III and V, as well as of motifs I and IV, in Prp28p are likely to be in close proximity to each other. Our results thus provide the first hint of the local structural arrangement for Prp28p, and perhaps for other DBPs as well.
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