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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2002.1
- 수록면
- 489 - 495 (7page)
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Deoxyhypusine synthase catalyzes the first step in the posttranslational synthesis of an unusual ami-no acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF-5A) precursor protein. We earlier observed that yeast recombinant deoxyhy-pusine synthase was phosphorylated by protein kinase C (PKC) in vitro (Kang and Chung, 1999) and the phosphorylation rate was synergistically increased to a 3.5-fold folowing treatment with phosphatidylserine (P.Ser)/diacylglycerol (DAG)/ Ca2+We have extended study on the phosphorylation of deoxyhypusine synthase in vivo in diferent cel lines in order to define its role on the regulation of eIF5A in the cel. Deoxyhypusine synthase was found to be phosphorylated by endogenous ki-nases in CHO, NIH3T3, and chicken embryonic cells. The highest degre of phosphorylation was found in CHO cels. Moreover, phosphorylation of deoxyhypusine synthase in intact CHO cels was revealed and the expression of phosphorylated deoxyhypusine synthase was significantly dimin-ished by diacyl ethylene glycol (DAEG), a PKC in-hibitor, and enhanced by phorbol 12-myristate 13-acetate (PMA) or Ca2+/DAG. Endogenous PKC in CHO cell and cell lysate was able to phosphorylate deoxyhypusine synthase and this modification is enhanced by PMA or Ca2+ plus DAG. Close asso-ciation of PKC with deoxyhypusine synthase in the CHO cells was evident in the immune copre-cipitation and was PMA-, and Ca2+/phospholipid-dependent. These results suggest that phosphory-lation of deoxyhypusine synthase was PKC-de-sible regulation in the interaction with eIF5A pre-cursor for hypusine synthesis.
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