1. V. R. Gerbasi, J. B. Preall, D. E. Golden, D. W. Powell, T. D. Cummins and E. J. Sontheimer (2011) Blanks, a nuclear siRNA/dsRNA-binding complex component, is required for Drosophila spermiogenesis. Proc Natl Acad Sci U S A 108(8): 3204-9.
Abstract Small RNAs and a diverse array of protein partners control gene expression in eukaryotes through a variety of mechanisms. By combining siRNA affinity chromatography and mass spectrometry, we have identified the double-stranded RNA-binding domain protein Blanks to be an siRNA- and dsRNA-binding protein from Drosophila S2 cells. We find that Blanks is a nuclear factor that contributes to the efficiency of RNAi. Biochemical fractionation of a Blanks-containing complex shows that the Blanks complex is unlike previously described RNA-induced silencing complexes and associates with the DEAD-box helicase RM62, a protein previously implicated in RNA silencing. In flies, Blanks is highly expressed in testes tissues and is necessary for postmeiotic spermiogenesis, but loss of Blanks is not accompanied by detectable transposon derepression. Instead, genes related to innate immunity pathways are up-regulated in blanks mutant testes. These results reveal Blanks to be a unique component of a nuclear siRNA/dsRNA-binding complex that contributes to essential RNA silencing-related pathways in the male germ line. PMID: [21300896]
2. E. Arama, M. Bader, M. Srivastava, A. Bergmann and H. Steller (2006) The two Drosophila cytochrome C proteins can function in both respiration and caspase activation. EMBO J 25(1): 232-43.
Abstract Cytochrome C has two apparently separable cellular functions PMID: [16362035]
Figures for illustrating the function of this protein/gene
Ref: V. R. Gerbasi, J. B. Preall, D. E. Golden, D. W. Powell, T. D. Cummins and E. J. Sontheimer (2011) Blanks, a nuclear siRNA/dsRNA-binding complex component, is required for Drosophila spermiogenesis. Proc Natl Acad Sci U S A 108(8): 3204-9. PMID: [21300896]
Function
Electron carrier protein. The oxidized form of thecytochrome c heme group can accept an electron from the heme groupof the cytochrome c1 subunit of cytochrome reductase. Cytochrome cthen transfers this electron to the cytochrome oxidase complex,the final protein carrier in the mitochondrial electron-transportchain.