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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2003.1
- 수록면
- 557 - 565 (9page)
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Deoxyhypusine is a modified lysine and formed postranslationaly to be the eukaryotic initiation factor eIF5A by deoxyhypusine synthase, employ-ing spermidine as butylamine donor. Subsequent hydroxylation of this deoxyhypusine-containing in-termediate completes the maturation of eIF5A. The previous report showed that deoxyhypusine synth-ase was phosphorylated by PKC in vivo and the association of deoxyhypusine synthase with PKC in CHO cels was PMA-, and Ca2+/phospholipid-de-pendent. We have extended study on the phos-phorylation of deoxyhypusine synthase by protein kinase CK2 in order to define its role on the re-gulation of eIF5A in the cell. The results showed that deoxyhypusine synthase was phosphorylated by CK2 in vivo as wel as in vitro. Endogenous CK2 in HeLa cells and the cell lysate was able to phosphorylate deoxyhypusine synthase and this modification is enhanced or decreased by the adi-tion of CK2 efectors such as polylysine, heparin, and poly(Glu, Tyr) 4:1. Phosphoamino acid analy-sis of this enzyme revealed that deoxyhypusine synthase is mainly phosphorylated on threonine residue and less intensely on serine. These results suggest that phosphorylation of deoxyhypusine synthase is CK2-dependent celular event as wel as PKC-mediated effect. However, there were no observable changes in enzyme activity betwen the phosphorylated and unphosphorylated forms of deoxyhypusine synthase. Taken together, be-sides its established function in hypusine modifi-synthase and its phosphorylation modification may have other independent celular functions because of versatile roles of deoxyhypusine synthase.
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