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PRP22 Prp22p

Prp22, Prp22p
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. This gene encodes a DEAD box protein, which is highly homologous to yeast Prp22. This protein facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PRP16, CAN, STEP, ACID, ATPase
Papers on Prp22
Incomplete splicing, cell division defects, and hematopoietic blockage in dhx8 mutant zebrafish.
Liu et al., Bethesda, United States. In Dev Dyn, 2012
dhx8 is the zebrafish ortholog of the yeast splicing factor prp22, which is a DEAH-box RNA helicase.
MRN1 implicates chromatin remodeling complexes and architectural factors in mRNA maturation.
Holmberg et al., Copenhagen, Denmark. In Plos One, 2011
Genetic interactions are observed between 2 µm-MRN1 and the splicing deficient mutants snt309Δ, prp3, prp4, and prp22, and additional genetic analyses link MRN1, SNT309, NHP6A/B, SWI/SNF, and RSC supporting the notion of a role of chromatin structure in mRNA processing.
Nonsense-mediated mRNA decay mutes the splicing defects of spliceosome component mutations.
Chanfreau et al., Los Angeles, United States. In Rna, 2009
Inactivation of Upf1p in the second step/recycling factor prp22-1 mutant and in the nam8Delta and mud1Delta U1 snRNP component mutants also increase unspliced precursor accumulation of several specific transcripts.
Crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of the human spliceosomal DExD/H-box protein hPrp22.
GeneRIF
Ficner et al., Göttingen, Germany. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009
Preliminary X-ray diffraction analysis of the crystals of the C-terminal domain of the human DExD/H-box protein hPrp22 at 2.1 A resolution, is reported.
Prp45 affects Prp22 partition in spliceosomal complexes and splicing efficiency of non-consensus substrates.
Půta et al., Praha, Czech Republic. In J Cell Biochem, 2009
Using a synthetic lethality screen, we found that prp45(1-169) genetically interacts with alleles of NTC members SYF1, CLF1/SYF3, NTC20, and CEF1, and 2nd step splicing factors SLU7, PRP17, PRP18, and PRP22.
Functional interactions between Prp8, Prp18, Slu7, and U5 snRNA during the second step of pre-mRNA splicing.
Schwer et al., New York City, United States. In Rna, 2007
After the second transesterification step of pre-mRNA splicing, the Prp22 helicase catalyzes release of spliced mRNA by disrupting contacts in the spliceosome that likely involve Prp8.
Exon ligation is proofread by the DExD/H-box ATPase Prp22p.
Staley et al., Chicago, United States. In Nat Struct Mol Biol, 2006
This proofreading activity is disabled by mutations that impair the ATPase or RNA unwindase activity of Prp22p, a conserved spliceosomal DExD/H-box ATPase.
Characterization of the NTPase, RNA-binding, and RNA helicase activities of the DEAH-box splicing factor Prp22.
GeneRIF
Schwer et al., New York City, United States. In Biochemistry, 2005
Prp22 unwinds duplexes with 3' overhangs; the 3' -> 5' directionality has implications for positioning of Prp22 on the RNA target
Motifs IV and V in the DEAH box splicing factor Prp22 are important for RNA unwinding, and helicase-defective Prp22 mutants are suppressed by Prp8.
Schwer et al., New York City, United States. In J Biol Chem, 2004
The yeast pre-mRNA splicing factor Prp22 is a member of the DEAH box family of nucleic acid-stimulated ATPases and RNA helicases.
Dependence of pre-mRNA introns on PRP17, a non-essential splicing factor: implications for efficient progression through cell cycle transitions.
Vijayraghavan et al., Bengaluru, India. In Nucleic Acids Res, 2003
TUB1 splicing is inefficient in prp17, prp16 and prp22, and marginally affected in prp18, slu7-1 and psf1-1.
Removal of a single alpha-tubulin gene intron suppresses cell cycle arrest phenotypes of splicing factor mutations in Saccharomyces cerevisiae.
Gould et al., Nashville, United States. In Mol Cell Biol, 2002
Removing the TUB1 intron from two other splicing mutants that arrest at G(2)/M, prp17Delta and prp22-1 strains, permits nuclear division, but suppression of the cell cycle block is less efficient.
Functional domains of the yeast splicing factor Prp22p.
Schwer et al., New York City, United States. In J Biol Chem, 2001
Here we delineate a minimal functional domain, Prp22(262-1145), that suffices for the activity of Prp22p in vivo when expressed under the natural PRP22 promoter and for pre-mRNA splicing activity in vitro.
Tracing the origin of the compensasome: evolutionary history of DEAH helicase and MYST acetyltransferase gene families.
Marín et al., Valencia, Spain. In Mol Biol Evol, 2001
The first branch includes the yeast PRP2, PRP16, PRP22, and PRP43 splicing factors and their orthologs in animal species.
RNA helicase dynamics in pre-mRNA splicing.
Meszaros et al., New York City, United States. In Embo J, 2001
The DExH-box NTPase/helicase Prp22p plays two important roles in pre-mRNA splicing.
The hermaphrodite sperm/oocyte switch requires the Caenorhabditis elegans homologs of PRP2 and PRP22.
Kimble et al., Madison, United States. In Proc Natl Acad Sci U S A, 2000
A phylogenetic analysis revealed that the C. elegans MOG-1, MOG-4, and MOG-5 proteins are closely related to the yeast proteins PRP16, PRP2, and PRP22, respectively.
Interaction of the yeast DExH-box RNA helicase prp22p with the 3' splice site during the second step of nuclear pre-mRNA splicing.
Muhlenkamp et al., Cleveland, United States. In Nucleic Acids Res, 2000
The other factor is the DExH-box RNA helicase, Prp22p.
Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes.
Impact
Abelson et al., Pasadena, United States. In Nature, 1991
The product of the yeast PRP22 gene acts late in the splicing of yeast pre-messenger RNA, mediating the release of the spliced mRNA from the spliceosome.
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