Biochemical and Biophysical Research Communications
The human Ski-interacting protein functionally substitutes for the yeast PRP45 gene
Section snippets
Materials and methods
Yeast strain and media. The yeast strain used was obtained from Research Genetics the genotype is MATa/αhis3Δ1/his3Δ1 leu2Δ/leu2Δ lys2Δ/LYS2 MET15/met15Δura3Δ/ura3Δ (4741/4742) PRP45/prp45Δ kanmx4. Media were prepared as described in [19].
Plasmid construction. The human Ski-interacting protein was cloned from pCS2Skip and digested with BamHI and XbaI, where the XbaI site was blunted. The insert was cloned into the yeast shuttle vector p426ADH [20] plasmid using a 5′BamHI and blunted 3′EcoRI
Amino acid alignment of Skip, Bx42, and Prp45 shows two regions of homology
Amino acid alignment of the polypeptide sequences of Skip from Homo sapiens (AAC15912.1), Bx42 from Drosophila melanogaster (P39736), and Prp45 from S. cerevisiae (NP_009370.1) is shown in Fig. 1. As can be seen there is a much greater degree of homology between the human and Drosophila proteins than there is with Prp45. This extensive homology is also seen with the Skip homologs from mouse, S. pombe and all the other Skip homologs described to date (data not shown). In marked contrast, Fig. 1
Acknowledgements
We thank Rolf Sternglanz for his help in writing the manuscript and the Sternglanz lab for providing reagents and technical assistance; Jean Beggs and Michael Albers for initial work that spurred these studies; K. Donnelly for supporting our research project; and all the members of our laboratory for helpful discussions and criticism. This work was supported by Grant CA42573 from the National Institutes of Health to M.J.H.
References (21)
- et al.
Integrating mRNA processing with transcription
Cell
(2002) - et al.
A unified theory of gene expression
Cell
(2002) - et al.
Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription
J. Biol. Chem.
(2001) - et al.
Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription
J. Biol. Chem.
(2001) - et al.
NCoA62/SKIP is a nuclear matrix-associated coactivator that may couple vitamin D receptor-mediated transcription and RNA splicing
J. Biol. Chem.
(2003) - et al.
The homolog of chromatin binding protein Bx42 identified in Dictyostelium
Gene
(1996) - et al.
The origin of the ankyrin repeat region in Notch intracellular domains is critical for regulation of HES promoter activity
Mech. Dev.
(2001) - et al.
Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
Gene
(1995) - et al.
Ski-interacting protein, a bifunctional nuclear receptor coregulator that interacts with N-CoR/SMRT and p300
Biochem. Biophys. Res. Commun.
(2004) - et al.
Alternative pre-mRNA splicing and proteome expansion in metazoans
Nature
(2002)
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2015, Molecular PlantCitation Excerpt :Prp45 is the SKIP homolog in yeast (Gahura et al., 2009). Weak prp45 alleles exhibit a temperature-sensitive growth phenotype, while strong prp45 alleles are lethal (Figueroa and Hayman, 2004; Gahura et al., 2009). Human SKIP is necessary for the expression of p21, and defects in SKIP result in subsequent p53-mediated apoptosis (Chen et al., 2011).
SKIP and BIR-1/Survivin have potential to integrate proteome status with gene expression
2014, Journal of ProteomicsCitation Excerpt :SKIP also directly binds the retinoblastoma tumor suppressor protein pRb and, in co-operation with Ski, overcomes the G1 arrest induced by pRb [45]. SKIP is also involved in regulation of splicing [12,13,46,47]. Thus, SKIP has a well-documented role in the regulation of transcription and cell cycle.
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The Role of Alternative Splicing During the Cell Cycle and Programmed Cell Death
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