Backbone assignment of the SARAH domain from Mst2 kinase

• Main Authors: Eunha Hwang, Maheswari Ethiraj, Chaejoon Cheong, Hae-Kap Cheong, Young Ho Jeon
• Format: Article
• Language: English
• Published: SpringerOpen 2010-03-01
• Series: Journal of Analytical Science and Technology
• Subjects: SARAH; Mst; Backbone assignment; NMR
• Online Access: http://www.jastmag.org/journal/view.php?number=10

Mst1 and Mst2 (Mammalian Sterile 20-like kinase 1 and 2) are pro-apoptotic protein kinases and involved in cell proliferation and survival. The C-termini of Mst1 and Mst contain a protein-protein interaction domain, named SARAH (Sav/Rassf/Hpo), which is found in three classes of eukaryotic tumour suppressors, Salvador, Rassf, and Hippo. The interaction of these SARAH domains controls apoptosis and cell cycle arrest. Moreover, Mst2 SARAH domain is known to interact with Raf-1, resulting in the suppression of apoptosis. In this study, we describe the sample preparation and NMR study of SARAH domain from Mst2 kinase. The gel-filtration chromatography shows that the SARAH domain of Mst2 forms a homodimer in solution. The NMR spectrum of Mst2 SARAH domain exhibit well-dispersed and homogeneous signals, which enable us to assign the backbone signals completely. These results provide a useful information for the structural and functional study of Mst2 SARAH domain.