Magdalena Spiechowicz

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In this work, we identified Hsp70 as a novel target of the Sgt1 protein. Using co-immunoprecipitation, affinity chromatography and ELISA we showed that, besides Hsp90, Sgt1 interacts with the heat shock protein, Hsp70. We also found that a deletion mutant of Sgt1, devoid of the C-terminal region, did not bind to either Hsp70 or Hsp90 proteins.(More)
Sgt1 was discovered as a protein required for the mitotic activity of kinetochore and for the activity of ubiquitin ligase in yeast [Kitagawa, K., Skowyra, D., Elledge, S.J., Harper, J.W., Hieter, P., 1999. SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex. Mol. Cell 4,(More)
S100A6 (calcyclin), a small calcium-binding protein from the S100 family, interacts with several target proteins in a calcium-regulated manner. One target is Calcyclin-Binding Protein/Siah-1-Interacting Protein (CacyBP/SIP), a component of a novel pathway of beta-catenin ubiquitination. A recently discovered yeast homolog of CacyBP/SIP, Sgt1, associates(More)
The Sgt1 protein was discovered in yeast but later it was found in other eucaryotic organisms, including plants and mammals. It was suggested that the Sgt1 protein plays a role in the CBF3 kinetochore and the SCF ubiquitin ligase complexes. Since the distribution, properties and functions of the mammalian Sgt1 have not been extensively studied, we examined(More)
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