Association and Phosphorylation of Deoxyhypusine Synthase with CK2


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Deoxyhypusine synthase (DHS) catalyzes the first step in the posttranslational synthesis of hypusine in the eukaryotic initiation factor 5A (eIF5A) precursor protein. As such, the phosphorylation of DHS by the protein kinase CK2 was investigated to define the role of DHS in the regulation of eIF5A in cells. The results showed that DHS was phosphorylated by CK2 in vivo as well as in vitro. The endogenous CK2 in HeLa cells and cell lysates was able to phosphorylate DHS and this modification was enhanced or decreased by the addition of CK2 effectors, such as polylysine, heparin, or poly (Glu, Tyr). A phosphoamino acid analysis of the enzyme revealed that the DHS was mainly phosphorylated into the Thr residue, with the remainder into the Ser residue. Therefore, it would appear that the phosphorylation of DHS was a CK2-dependent cellular event, thereby opening the path for possible regulation of the interaction with the eIF5A precursor for hypusine synthesis.



Key Engineering Materials (Volumes 277-279)

Edited by:

Kwang Hwa Chung, Yong Hyeon Shin, Sue-Nie Park, Hyun Sook Cho, Soon-Ae Yoo, Byung Joo Min, Hyo-Suk Lim and Kyung Hwa Yoo




K. R. Kang, "Association and Phosphorylation of Deoxyhypusine Synthase with CK2", Key Engineering Materials, Vols. 277-279, pp. 102-106, 2005

Online since:

January 2005





[1] M.H. Park, H.L. Cooper and J.E. Folk: J. Biol. Chem. Vol. 257 (1982), pp.7217-22.

[2] A. Abbruzzese, V. Liguori and M.H. Park: Adv. Exp. Med. Biol. Vol. 250 (1988), pp.459-66.

[3] H.A. Kang, H.G. Schwelberger and J.W. Hershey: J. Biol. Chem. Vol. 268 (1993), pp.14750-6.

[4] T. Hunter: Cell Vol. 100 (2000), pp.113-27.

[5] L.A. Pinna: Biochim. Biophys. Acta Vol. 1054 (1990), pp.267-84.

[6] F. Meggio, O. Marin and L.A. Pinna: Cell. Mol. Biol. Res. Vol. 40 (1994), pp.401-9.

[7] K.R. Kang and S.I. Chung: Exp. Mol. Med. Vol. 31 (1999), pp.210-6.

[8] K.R. Kang, J.S. Kim, S.I. Chung, M.H. Park, Y.W. Kim, D. Lim and S.Y. Lee: Exp. Mol. Med. Vol. 34 (2002), pp.489-95.

[9] M.H. Park, E.C. Wolff and J.E. Folk: Biofactors Vol. 4(1993), pp.95-104.

[10] F. Meggio, B. Boldyreff, O.G. Issinger and L.A. Pinna: Biochemistry Vol. 33 (1994), pp.4336-42.

[11] D. Ober and T. Hartmann: J. Biol. Chem. Vol. 274 (1999), pp.32040-7.

[12] M.H. Park, Y.A. Joe and K.R. Kang: J. Biol. Chem. Vol. 273 (1998), pp.1677-83.

[13] D. Ober and T. Hartmann: Proc. Natl. Acad. Sci. USA Vol. 96 (1999), pp.14777-82.

[14] S. Ramaswamy, K.N. Ross, E.S. Lander and T.R. Golub: Nat. Genet. Vol. 33 (2003), pp.49-54.