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SNU114 Snu114p

Snu114p, Snu114
This gene encodes a GTPase which is a component of the spliceosome complex which processes precursor mRNAs to produce mature mRNAs. Mutations in this gene are associated with mandibulofacial dysostosis with microcephaly. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Apr 2012] (from NCBI)
Top mentioned proteins: Elongation Factor 2, STEP, ATPase, PRP28, CAN
Papers on Snu114p
Cwc21p promotes the second step conformation of the spliceosome and modulates 3' splice site selection.
New
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.
Haploinsufficiency of a spliceosomal GTPase encoded by EFTUD2 causes mandibulofacial dysostosis with microcephaly.
GeneRIF
Boycott et al., Ottawa, Canada. In Am J Hum Genet, 2012
Validation studies of eight additional individuals with MFDM demonstrated causative EFTUD2 mutations in all affected individuals tested.
Physical and genetic interactions of yeast Cwc21p, an ortholog of human SRm300/SRRM2, suggest a role at the catalytic center of the spliceosome.
Beggs et al., Edinburgh, United Kingdom. In Rna, 2009
Here, we show that Cwc21p binds directly to two key splicing factors-namely, Prp8p and Snu114p-and becomes the first NTC-related protein known to dock directly to U5 snRNP proteins.
Analysis of synthetic lethality reveals genetic interactions between the GTPase Snu114p and snRNAs in the catalytic core of the Saccharomyces cerevisiae spliceosome.
GeneRIF
O'Keefe et al., Manchester, United Kingdom. In Genetics, 2009
Data suggest that the RNA base pairing state is directly or indirectly sensed by the Snu114p G domain.
VAJ/GFA1/CLO is involved in the directional control of floral organ growth.
Okada et al., Kyoto, Japan. In Plant Cell Physiol, 2009
The VAJ/GFA1/CLO gene encodes a translational elongation factor-2 (EF-2) family protein, of which the human U5-116 kD and yeast Snu114p counterparts are U5 small nuclear ribonucleoprotein (snRNP)-specific proteins.
Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-snRNP by electron microscopy.
GeneRIF
Lührmann et al., Göttingen, Germany. In Nat Struct Mol Biol, 2008
Results report the structure of the Saccharomyces cerevisiae tri-snRNP, and show that U4/U6 snRNP forms a domain termed the arm, while a separate head domain adjacent to the arm harbors Brr2, and Prp8 and the GTPase Snu114 are located centrally.
The role of Snu114p during pre-mRNA splicing.
Review
O'Keefe et al., Manchester, United Kingdom. In Biochem Soc Trans, 2008
The spliceosome protein Snu114p is a GTPase that is related to the translation elongation factor EF-2. Snu114p plays a key role in spliceosome remodelling.
The EF-G-like GTPase Snu114p regulates spliceosome dynamics mediated by Brr2p, a DExD/H box ATPase.
GeneRIF
Staley et al., Chicago, United States. In Mol Cell, 2006
Snu114p serves as a signal-dependent switch that transduces signals to Brr2p to control spliceosome dynamics.
Assembly of Snu114 into U5 snRNP requires Prp8 and a functional GTPase domain.
GeneRIF
Guthrie et al., San Francisco, United States. In Rna, 2006
Assembly of Snu114 into U5 snRNP requires Prp8 and a functional GTPase domain.
Prp8p dissection reveals domain structure and protein interaction sites.
GeneRIF
Beggs et al., Edinburgh, United Kingdom. In Rna, 2006
Prp8 interaction site with Snu114 protein
Genetic analysis reveals a role for the C terminus of the Saccharomyces cerevisiae GTPase Snu114 during spliceosome activation.
GeneRIF
Guthrie et al., San Francisco, United States. In Genetics, 2005
GTP hydrolysis results in a rearrangement between Prp8 and the C terminus of Snu114 that leads to release of U1 and U4, thus activating the spliceosome for catalysis.
Mutagenesis suggests several roles of Snu114p in pre-mRNA splicing.
Fabrizio et al., Göttingen, Germany. In J Biol Chem, 2003
Snu114p, a yeast U5 small nuclear ribonucleoprotein (snRNP) homologous to the ribosomal GTPase EF-2, was recently found to play a part in the dissociation of U4 small nuclear RNA (snRNA) from U6 snRNA.
The Clf1p splicing factor promotes spliceosome assembly through N-terminal tetratricopeptide repeat contacts.
Rymond et al., Lexington, United States. In J Biol Chem, 2003
Clf1Delta2-TAP) destabilizes Clf1p complexes assembled in vivo, causing the release of the Cef1p and Prp19p NTC factors and decreased association of the Rse1p, Snu114p, and Hsh155p snRNP proteins.
The ribosomal translocase homologue Snu114p is involved in unwinding U4/U6 RNA during activation of the spliceosome.
Fabrizio et al., Göttingen, Germany. In Embo Rep, 2002
Snu114p is a yeast U5 snRNP protein homologous to the ribosomal elongation factor EF-2. Snu114p exhibits the same domain structure as EF-2, including the G-domain, but with an additional N-terminal domain.
The yeast U5 snRNP coisolated with the U1 snRNP has an unexpected protein composition and includes the splicing factor Aar2p.
Fabrizio et al., Göttingen, Germany. In Rna, 2001
In addition to the Sm core proteins, it contains only two of the U5 snRNP specific proteins, Prp8p and Snu114p.
Protein-RNA interactions in the U5 snRNP of Saccharomyces cerevisiae.
Beggs et al., Edinburgh, United Kingdom. In Rna, 1998
Photo-crosslinking with uniformly labeled U5 RNA in snRNPs reconstituted in vitro revealed five contacting proteins, Prp8p, Snu114p, p30, p16, and p10, contact by the three smaller proteins requiring an intact Sm site.
Protein-RNA interactions in the U5 snRNP of Saccharomyces cerevisiae.
Beggs et al., Edinburgh, United Kingdom. In Rna, 1998
Photo-crosslinking with uniformly labeled U5 RNA in snRNPs reconstituted in vitro revealed five contacting proteins, Prp8p, Snu114p, p30, p16, and p10, contact by the three smaller proteins requiring an intact Sm site.
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