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PRP11 Prp11p

PRP11, RNA11, Prp11p, SF3a66
This gene encodes subunit 2 of the splicing factor 3a protein complex. The splicing factor 3a heterotrimer includes subunits 1, 2 and 3 and is necessary for the in vitro conversion of 15S U2 snRNP into an active 17S particle that performs pre-mRNA splicing. Subunit 2 interacts with subunit 1 through its amino-terminus while the single zinc finger domain of subunit 2 plays a role in its binding to the 15S U2 snRNP. Subunit 2 may also function independently of its RNA splicing function as a microtubule-binding protein. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PRP9, PRP21, CAN, PrP, ACID
Papers on PRP11
The complete mitochondrial genome sequence of Hepatozoon catesbianae (Apicomplexa: Coccidia: Adeleorina), a blood parasite of the green frog, Lithobates (formerly Rana) clamitans.
Barta et al., Guelph, Canada. In J Parasitol, 2014
Sequences corresponding to rDNA fragments RNA5, RNA8, RNA11, and RNA19 of Plasmodium falciparum were not identified in the mitrochondrial genome sequence of H. catesbianae.
Physicochemical analysis of rotavirus segment 11 supports a 'modified panhandle' structure and not the predicted alternative tRNA-like structure (TRLS).
Lever et al., Cambridge, United Kingdom. In Arch Virol, 2014
Covariation studies and phylogenetic analysis exploring the potential structure of RNA11 of rotaviruses suggested that, besides the previously predicted "modified panhandle" structure, the 5' and 3' termini of one of the isoforms of the bovine rotavirus UKtc strain may interact to form a tRNA-like structure (TRLS).
Proteins associated with SF3a60 in T. brucei.
Levin et al., Buenos Aires, Argentina. In Plos One, 2013
The interactions with SF3a120, SF3a66 and SAP130 were confirmed by tandem affinity purification and mass spectrometry.
A semi-dominant mutation in the general splicing factor SF3a66 causes anterior-posterior axis reversal in one-cell stage C. elegans embryos.
Bowerman et al., Eugene, United States. In Plos One, 2013
Here we show that a semi-dominant mutation in the general splicing factor SF3a66 can lead to a reversed axis of AP polarity that depends on PAR-2 and possibly on close proximity of oocyte meiotic spindles with the cell cortex.
Competition between pre-mRNAs for the splicing machinery drives global regulation of splicing.
Ares et al., Santa Cruz, United States. In Mol Cell, 2013
Downregulation of the RPG-dedicated transcription factor gene IFH1 genetically suppresses two spliceosome mutations, prp11-1 and prp4-1, and globally restores splicing efficiency in prp4-1 cells.
Interaction domains and nuclear targeting signals in subunits of the U2 small nuclear ribonucleoprotein particle-associated splicing factor SF3a.
Krämer et al., Genève, Switzerland. In J Biol Chem, 2011
Our results indicate that the SF3a66-SF3a120 interaction is mediated by a 27-amino acid region in SF3a120 C-terminal to the second suppressor-of-white-apricot and prp21/spp91 domain and amino acids 108-210 of SF3a66.
Genomic analysis of codon, sequence and structural conservation with selective biochemical-structure mapping reveals highly conserved and dynamic structures in rotavirus RNAs with potential cis-acting functions.
Lever et al., Cambridge, United Kingdom. In Nucleic Acids Res, 2010
Biochemical structural analysis of RNA11 confirmed the presence of terminal LRIs and two internal helices with high codon and sequence conservation.
Interaction of yeast eIF4G with spliceosome components: implications in pre-mRNA processing events.
Lewis et al., Edinburgh, United Kingdom. In Rna Biol, 2009
In addition, Tif4631p and Tif4632p associate with protein components of the splicing machinery, namely Snu71p and Prp11p.
Spp382p interacts with multiple yeast splicing factors, including possible regulators of Prp43 DExD/H-Box protein function.
Rymond et al., Lexington, United States. In Genetics, 2009
Identified, among others, are genes encoding the established splicing factors Prp8p, Prp9p, Prp11p, Prp39p, and Yhc1p and two poorly characterized proteins with possible links to splicing, Sqs1p and Cwc23p.
A WW-like module in the RAG1 N-terminal domain contributes to previously unidentified protein-protein interactions.
Sadofsky et al., New York City, United States. In Nucleic Acids Res, 2009
We confirmed the interaction already described with KPNA2/RCH1/SRP1alpha and found two others--to the transcription factor GMEB1/PIF p96 and the splicing factor SF3A2/SF3a66.
Structure-function analysis of the U2 snRNP-associated splicing factor SF3a.
Tanackovic et al., Genève, Switzerland. In Biochem Soc Trans, 2005
Studies aimed at the identification of regions in SF3a60 and SF3a66, required for proper intracellular localization, have led to a model for the final steps in U2 snRNP biogenesis and the proposal that SF3a is incorporated into the U2 snRNP in Cajal bodies.
Human splicing factor SF3a, but not SF1, is essential for pre-mRNA splicing in vivo.
Krämer et al., Genève, Switzerland. In Mol Biol Cell, 2005
SF3a60, 66, and 120, but not SF1, are essential for pre-mRNA splicing
Interaction between PRP11 and SPP91 yeast splicing factors and characterization of a PRP9-PRP11-SPP91 complex.
Chapon et al., Paris, France. In Science, 1993
Here it is demonstrated that protein-protein interactions occur between SPP91 and PRP11.
Correspondence between a mammalian spliceosome component and an essential yeast splicing factor.
Reed et al., Boston, United States. In Science, 1993
It is demonstrated that SAP 62 is the likely functional homolog of the yeast PRP11 protein.
The yeast RNA gene products are essential for mRNA splicing in vitro.
Abelson et al., In Cell, 1987
The yeast rna mutations (rna2-rna11) are a set of temperature-sensitive mutations that result in the accumulation of intron-containing mRNA precursors at the restrictive temperature.
Genetic Mapping of the pho2, PHO82-pho4 and pho85 Loci of Yeast.
Toh-E, Bethesda, United States. In Genetics, 1980
The pho2 locus was 40 cM from rna11 on the left arm of chromosome IV.
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