Disease relevance of Sptr

• The protein-coding region of the cDNA was expressed in Escherichia coli as a histidine fusion protein, and the resulting recombinant protein proved to have SR activity [1].

High impact information on Sptr

• Splicing factors of the SR protein family play a major role in this regulation, as they are required for early recognition of splice sites during spliceosome assembly [2].
• These results demonstrate that a SR protein kinase plays a specific role in developmentally regulated alternative splicing [3].
• Negative autoregulation of SR proteins has been proposed to exert homeostatic control on the splicing environment, but few examples have been studied and the role of isoforms that lack the RS domain is unclear [4].
• These differential and specific effects of SR proteins indicate that they function to confer accuracy to developmental gene expression programs by facilitating the cell lineage decisions that underline the generation of tissue identities [5].
• Modulating the expression levels of five SR proteins in the developing eye of Drosophila melanogaster revealed that these splicing factors induce various phenotypic alterations in eye organogenesis and also affect viability [5].

Biological context of Sptr

• The Drosophila SR gene maps to 15A on the X chromosome [6].
• Ammonium sulfate fractionation and standard column chromatography techniques have been used to purify the enzyme sepiapterin reductase to electrophoretic homogeneity from pupae of Drosophila melanogaster [7].
• The active site residues proposed from the three-dimensional structure of mouse SR are well conserved in Drosophila SR [1].
• Genetic enhancement of RNA-processing defects by a dominant mutation in B52, the Drosophila gene for an SR protein splicing factor [8].
• The observation that a nonfunctional version of the FP enhancer (FPD) that does not bind SF2/ASF also fails to block splicing when paired with the NRS 3' region supports the notion that SF2/ASF binding to the NRS is relevant, but other SR proteins may substitute if an appropriate binding site is supplied [9].

Associations of Sptr with chemical compounds

• Sepiapterin reductase and the biosynthesis of tetrahydrobiopterin in Drosophila melanogaster [7].
• It appears that although purified Drosophila sepiapterin reductase can catalyze low levels of conversion of 6-pyruvoyltetrahydropterin (pyruvoyl-H4pterin) to H4 biopterin in the presence of NADPH, the efficient conversion of pyruvoyl-H4pterin to H4biopterin requires the presence of both sepiapterin reductase and pyruvoyl-H4pterin reductase [7].
• The SR activity of the recombinant protein was inhibited by two indoleamines, N-acetyl serotonin and melatonin [1].
• N-acetyldopamine, N-acetylserotonin, and N-methoxyacetylserotonin have shown to be noncompetitive inhibitors for the Drosophila sepiapterin reductase [10].

References