gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

PRP16 Prp16p

PRP16, Prp16p
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 member of the DEAD/H box family of splicing factors. This protein resembles yeast Prp16 more closely than other DEAD/H family members. It is an ATPase and essential for the catalytic step II in pre-mRNA splicing process. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: STEP, ATPase, Prp22, CAN, 9G8
Papers on PRP16
The Arabidopsis ortholog of the DEAH-box ATPase Prp16 influences auxin-mediated development.
Terada et al., Kyoto, Japan. In Plant Signal Behav, Nov 2015
In animals and yeasts, the DEAH-box RNA-dependent ATPase Prp16 facilitates pre-mRNA splicing.
Cwc21p promotes the second step conformation of the spliceosome and modulates 3' splice site selection.
Beggs et al., Barcelona, Spain. In Nucleic Acids Res, May 2015
Here, we show that mutations in PRP16, PRP8, SNU114 and the U5 snRNA that affect this process interact genetically with CWC21, that encodes the yeast orthologue of the human SR protein, SRm300/SRRM2.
CLUMSY VEIN, the Arabidopsis DEAH-box Prp16 ortholog, is required for auxin-mediated development.
Okada et al., Kyoto, Japan. In Plant J, 2015
In animals and yeasts, the DEAH-box RNA-dependent ATPase Prp16 mediates conformational change of the spliceosome, thereby facilitating pre-mRNA splicing.
Brr2p carboxy-terminal Sec63 domain modulates Prp16 splicing RNA helicase.
Beggs et al., Edinburgh, United Kingdom. In Nucleic Acids Res, 2015
Using genetic and biochemical approaches, we investigated interaction of the carboxy-terminal helicase module, in particular the carboxy-terminal Sec63-2 domain, with the splicing RNA helicase Prp16p.
A missense mutation in the splicing factor gene DHX38 is associated with early-onset retinitis pigmentosa with macular coloboma.
Cremers et al., Nijmegen, Netherlands. In J Med Genet, 2014
CONCLUSIONS: By combining genome-wide homozygosity mapping and exome sequencing, a novel missense mutation was identified in the DHX38 gene that encodes the pre-mRNA splicing factor PRP16, in a Pakistani family with early-onset autosomal-recessive RP.
Remodeling of U2-U6 snRNA helix I during pre-mRNA splicing by Prp16 and the NineTeen Complex protein Cwc2.
O'Keefe et al., Manchester, United Kingdom. In Nucleic Acids Res, 2014
The ATPase Prp16 remodels the spliceosome between the first and second steps of splicing by catalyzing release of first step factors Yju2 and Cwc25 as well as destabilizing U2-U6 snRNA helix I. How Prp16 destabilizes U2-U6 helix I is not clear.
Plasmodium falciparum Prp16 homologue and its role in splicing.
Malhotra et al., New Delhi, India. In Biochim Biophys Acta, 2012
Further we show by complementation assay in yeast that a chimeric yeast-Plasmodium Prp16 protein, not the full length PfPrp16, can rescue the yeast prp16 temperature-sensitive mutant.
The DEAH box ATPases Prp16 and Prp43 cooperate to proofread 5' splice site cleavage during pre-mRNA splicing.
Staley et al., Chicago, United States. In Mol Cell, 2010
The DEAH box ATPases Prp16 and Prp43 cooperate to proofread 5' splice site cleavage during pre-mRNA splicing.
Evidence that U2/U6 helix I promotes both catalytic steps of pre-mRNA splicing and rearranges in between these steps.
Staley et al., Chicago, United States. In Rna, 2009
Further, mutations that we proved weaken only U2/U6 helix I suppressed a mutation in PRP16, a DEAH-box ATPase required after 5' splice site cleavage, providing persuasive evidence that helix I is destabilized by Prp16p and suggesting that this structure is unwound between the catalytic steps.
Opposing classes of prp8 alleles modulate the transition between the catalytic steps of pre-mRNA splicing.
Konarska et al., New York City, United States. In Nat Struct Mol Biol, 2007
On the basis of genetic interactions, we propose that prp8-mediated substrate repositioning during the transition occurs between catalytic-center opening and closure mediated by the U6 small nuclear RNA and the DExH/D ATPase gene prp16.
U2 toggles iteratively between the stem IIa and stem IIc conformations to promote pre-mRNA splicing.
Staley et al., Chicago, United States. In Genes Dev, 2007
The prp16 mutation was also suppressed by mutations flanking stem IIc, suggesting that Prp16p facilitates a switch from stem IIc to the mutually exclusive U2 stem IIa, which activates binding of U2 to pre-mRNA during assembly.
Rearrangement of competing U2 RNA helices within the spliceosome promotes multiple steps in splicing.
Ares et al., Santa Cruz, United States. In Genes Dev, 2007
A second, later role for stem IIa is revealed by its suppression of a cold-sensitive allele of the second-step splicing factor PRP16.
The Isy1p component of the NineTeen complex interacts with the ATPase Prp16p to regulate the fidelity of pre-mRNA splicing.
Guthrie et al., San Francisco, United States. In Genes Dev, 2005
Prp16 remodels an interaction involving Isy1 in the transition between two steps of splicing
A mechanism to enhance mRNA splicing fidelity: the RNA-dependent ATPase Prp16 governs usage of a discard pathway for aberrant lariat intermediates.
Guthrie et al., San Francisco, United States. In Cell, 1993
PRP16 encodes an RNA-dependent ATPase required for the second step of mRNA splicing in S. cerevisiae.
Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes.
Abelson et al., Pasadena, United States. In Nature, 1991
The predicted PRP22 protein sequence shares extensive homology with that of PRP2 and PRP16 proteins, which are also involved in nuclear pre-mRNA splicing.
PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome.
Guthrie et al., San Francisco, United States. In Nature, 1991
The splicing factor PRP16 contains variations of several motifs that define the eIF-4A-like ATP-dependent RNA helicase family.
A putative ATP binding protein influences the fidelity of branchpoint recognition in yeast splicing.
Guthrie et al., San Francisco, United States. In Cell, 1990
We have now cloned the genomic region encoding the prp16-1 suppressor function and have demonstrated that PRP16 is essential for viability.
share on facebooktweetadd +1mail to friends