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Nucleic Acids Research, 2000, Vol. 28, No. 5 E14-e14
© 2000 Oxford University Press

Functional coexpression of serine protein kinase SRPK1 and its substrate ASF/SF2 in Escherichia coli

Bai-Gong Yue, Paul Ajuh1, Göran Akusjärvi, Angus I. Lamond1 and Jan-Peter Kreivi*

Department of Medical Biochemistry and Microbiology, Unit of Microbiology, Uppsala University, Box 582, S-751 23 Uppsala, Sweden and 1Department of Biochemistry, The University of Dundee, MSI/WTB Complex, Dow Street, Dundee DD1 5EH, UK

Mammalian proteins expressed in Escherichia coli are used in a variety of applications. A major drawback in producing eukaryotic proteins in E.coli is that the bacteria lack most eukaryotic post-translational modification systems, including serine/threonine protein kinase(s). Here we show that a eukaryotic protein can be phosphorylated in E.coli by simul­taneous expression of a mammalian protein kinase and its substrate. We show that in bacteria expressing SRPK1, ASF/SF2 becomes phosphorylated to a degree resembling native ASF/SF2 present in interphase HeLa cell nuclei. The E.coli phosphorylated ASF/SF2 is functional in splicing and, contrary to the unphosphorylated protein, soluble under native conditions.

* To whom correspondence should be addressed. Tel: +46 18 471 44 68; Fax: +46 18 509 876; Email: jan-peter.kreivi@imim.uu.se Permanent address: Bai-Gong Yue, Henan Bioproduct Institute, 9 Tongle Road, 450053 Zhengzhou, China


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