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Gene Review:

PRP31 - Prp31p

Saccharomyces cerevisiae S288c

Synonyms: Pre-mRNA-processing factor 31, YGR091W

Weidenhammer, E.M. et al., Hickey, A.J. et al., Mochizuki, H. et al., Kuhn, A.N. et al., Weidenhammer, E.M. et al.

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High impact information on PRP31

Furthermore, additional genetic interactions with U4-cs1 support a two-state model for this RNA conformational switch and implicate another splicing factor, Prp31, in Prp8-mediated spliceosome activation [1].
Prp31p promotes the association of the U4/U6 x U5 tri-snRNP with prespliceosomes to form spliceosomes in Saccharomyces cerevisiae [2].
Nondenaturing gel electrophoresis and glycerol gradient analyses demonstrate that while Prp31p may play a role in maintaining the assembly or stability of tri-snRNPs, functional protein is not essential for the formation of U4/U6 or U4/U6 x U5 snRNPs [2].
The wild-type PRP31 gene was cloned and shown to be essential for cell viability [3].
Although more reliable etiological mutations of RP11 were subsequently discovered in a human homologue of yeast pre-mRNA splicing gene (PRP31), the role of this R659S missense change in the pathogenicity of RP11 is still controversial [4].

Other interactions of PRP31

The protein with 234aa (named PrpM) was most similar to the putative protein Prp31p from Methanobacterium thermoautotrophicum, while the 193-aa protein (named FibM) was identified as an archaeal fibrillarin homolog [5].
The M. mazeii PrpM was also similar to three proteins from Saccharomyces cerevisiae: Prp31p, Nop56p, and Nop58p [5].

References

Distinct domains of splicing factor Prp8 mediate different aspects of spliceosome activation. Kuhn, A.N., Reichl, E.M., Brow, D.A. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
Prp31p promotes the association of the U4/U6 x U5 tri-snRNP with prespliceosomes to form spliceosomes in Saccharomyces cerevisiae. Weidenhammer, E.M., Ruiz-Noriega, M., Woolford, J.L. Mol. Cell. Biol. (1997) [Pubmed]
The PRP31 gene encodes a novel protein required for pre-mRNA splicing in Saccharomyces cerevisiae. Weidenhammer, E.M., Singh, M., Ruiz-Noriega, M., Woolford, J.L. Nucleic Acids Res. (1996) [Pubmed]
R659S mutation of gammaPKC is susceptible to cell death: Implication of this mutation/polymorphism in the pathogenesis of retinitis pigmentosa. Mochizuki, H., Seki, T., Adachi, N., Saito, N., Mishima, H.K., Sakai, N. Neurochem. Int. (2006) [Pubmed]
Identification of genes in the genome of the archaeon Methanosarcina mazeii that code for homologs of nuclear eukaryotic molecules involved in RNA processing. Hickey, A.J., Macario, A.J., Conway de Macario, E. Gene (2000) [Pubmed]

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