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PRP28 Prp28p

PRP28, Prp28p, U5-100kD
This gene encodes a member of the DEAD box protein family. DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure, such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. The protein encoded by this gene is a component of the U5 snRNP complex; it may facilitate conformational changes in the spliceosome during nuclear pre-mRNA splicing. An alternatively spliced transcript variant has been found for this gene, but its biological validity has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: STEP, ACID, ATPase, UIC, CAN
Papers on PRP28
A novel function for the DEAD-box RNA helicase DDX-23 in primary microRNA processing in Caenorhabditis elegans.
New
Chan et al., Taipei, Taiwan. In Dev Biol, Dec 2015
In a let-7(mg279) sensitized genetic background, knockdown of a homolog of yeast splicing factor Prp28p, DDX-23, or a homolog of human helicases p68 and p72, DDX-17, enhanced let-7 loss-of-function phenotypes, suggesting that these helicases play a role in let-7 processing and/or function.
An unanticipated early function of DEAD-box ATPase Prp28 during commitment to splicing is modulated by U5 snRNP protein Prp8.
Brow et al., In Rna, 2014
Catalytic activation requires the exchange of U6 for U1 snRNA at the 5' splice site, which is promoted by the DEAD-box protein Prp28.
Splicing proofreading at 5' splice sites by ATPase Prp28p.
Xu et al., Shanghai, China. In Nucleic Acids Res, 2013
Through a series of yeast genetic screens, we isolated alleles of prp28 that improve splicing of suboptimal 5'SS substrates, demonstrating that WT-Prp28p proofreads, and consequently rejects, poor 5'SS.
A targeted bypass screen identifies Ynl187p, Prp42p, Snu71p, and Cbp80p for stable U1 snRNP/Pre-mRNA interaction.
Chang et al., Columbus, United States. In Mol Cell Biol, 2009
To understand how DEXD/H-box proteins recognize and interact with their cellular substrates, we have been studying Prp28p, a DEXD/H-box splicing factor required for switching the U1 snRNP with the U6 snRNP at the precursor mRNA (pre-mRNA) 5' splice site.
The Caenorhabditis elegans DDX-23, a homolog of yeast splicing factor PRP28, is required for the sperm-oocyte switch and differentiation of various cell types.
Sugimoto et al., Kōbe, Japan. In Dev Dyn, 2008
Here we report the developmental function of a DEAD-box protein, DDX-23, in Caenorhabditis elegans, which has significant homology with the yeast splicing factor PRP28.
Phosphorylation of human PRP28 by SRPK2 is required for integration of the U4/U6-U5 tri-snRNP into the spliceosome.
GeneRIF
Lührmann et al., Göttingen, Germany. In Nat Struct Mol Biol, 2008
SRPK2 knock down results in hypophosphorylation of the arginine-serine (RS) domain-containing human PRP28 protein (PRP28, also known as DDX23), and destabilizes PRP28 association with the tri-snRNP.
Assembly of Snu114 into U5 snRNP requires Prp8 and a functional GTPase domain.
Guthrie et al., San Francisco, United States. In Rna, 2006
We recently identified allele-specific genetic interactions between SNU114 and genes encoding three other U5 snRNP components, Prp8 and two RNA-dependent ATPases, Prp28 and Brr2, required for destabilization of U1 and U4 snRNPs prior to catalysis.
Genetic analysis reveals a role for the C terminus of the Saccharomyces cerevisiae GTPase Snu114 during spliceosome activation.
Guthrie et al., San Francisco, United States. In Genetics, 2005
The allele snu114-60, which truncates the C terminus, was synthetically lethal with factors required for activation of the spliceosome, including the DExD/H-box ATPases BRR2 and PRP28.
Effects of the U1C L13 mutation and temperature regulation of yeast commitment complex formation.
Rosbash et al., Waltham, United States. In Proc Natl Acad Sci U S A, 2004
Mutations of amino acid L13 within this domain rescue the essential function of the helicase protein Prp28p.
Specific alterations of U1-C protein or U1 small nuclear RNA can eliminate the requirement of Prp28p, an essential DEAD box splicing factor.
Chang et al., Columbus, United States. In Mol Cell, 2001
Here, we show that the function of an otherwise essential DEAD box protein, Prp28p, can be bypassed by mutations that alter either the protein U1-C or the U1 small nuclear RNA.
An RNA switch at the 5' splice site requires ATP and the DEAD box protein Prp28p.
Guthrie et al., San Francisco, United States. In Mol Cell, 1999
Using genetics, we identified the DExD/H box protein Prp28p as a potential mediator of the switch.
The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro.
Lührmann et al., Marburg an der Lahn, Germany. In Proc Natl Acad Sci U S A, 1998
We recently have shown that spliceosomal U5 small nuclear ribonucleoproteins (snRNPs) from HeLa cells contain two proteins, U5-200kD and U5-100kD, which share homology with the DEAD/DEXH-box families of RNA helicases.
Genetic interactions of conserved regions in the DEAD-box protein Prp28p.
Abbott et al., Columbus, United States. In Nucleic Acids Res, 1998
Prp28p, the gene product of PRP28 , is a member of the evolutionarily conserved DEAD-box proteins (DBPs).
The human U5 snRNP-specific 100-kD protein is an RS domain-containing, putative RNA helicase with significant homology to the yeast splicing factor Prp28p.
Lührmann et al., Marburg an der Lahn, Germany. In Rna, 1997
A database homology search revealed a significant degree of homology (60% similarity, 37% identity) between the Saccharomyces cerevisiae splicing factor, Prp28p, which lacks an N-terminal RS domain, and the C-terminal domain of U5-100kD.
Identification of novel genes required for yeast pre-mRNA splicing by means of cold-sensitive mutations.
Guthrie et al., San Francisco, United States. In Genetics, 1996
Four of these affected known genes (PRP8, PRP16, PRP22, PRP28), three of which encode RNA helicase homologues.
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