Abstract
Signal Transducer and Activator of Transcription (STAT) proteins are latent cytoplasmic transcription factors that become activated by phosphorylation at a C-terminal tyrosine residue. Upon activation STAT proteins translocate to the nucleus and bind to their specific target sites. Here, we describe the recombinant expression of tyrosine phosphorylated STAT proteins in bacteria. This method allows the production of large amounts of activated STAT proteins for structural and biochemical studies including the high-throughput screening of chemical libraries.
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Acknowledgments
We thank former lab members Stefan Becker, Montserrat Soler-Lopez, and Carlo Petosa for setting up the initial protocols for STAT3β and Dd-STATa.
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Baudin, F., Müller, C.W. (2013). Bacterial Expression, Purification, and Crystallization of Tyrosine Phosphorylated STAT Proteins. In: Nicholson, S., Nicola, N. (eds) JAK-STAT Signalling. Methods in Molecular Biology, vol 967. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-242-1_21
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DOI: https://doi.org/10.1007/978-1-62703-242-1_21
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