| Literature DB >> 16430890 |
Masato Enomoto1, Yoshitaka Sawano, Seiji Kosuge, Yuko Yamano, Kazuyuki Kuroki, Kenzo Ohtsuki.
Abstract
Two alpha-type CK2-activated PKAs (CK2-aPKAIalpha and CK2-aPKAIIalpha) were biochemically characterized in vitro using GST-HBV core fusion protein (GST-Hcore) and GST-Hcore157B as phosphate acceptors. It was found that (i), in the absence of cAMP, these two CK2-aPKAs phosphorylated both Ser-170 and Ser-178 on GST-Hcore and Hcore157B; (ii) this phosphorylation was approx. 4-fold higher than their phosphorylation by cAMP-activated PKAs; and (iii) suramin effectively inhibited the phosphorylation of Hcore157B by CK2-aPKAIIalpha through its direct binding to Hcore157B in vitro. These results suggest that high phosphorylation of HBV-CP by two CK2-aPKAs, in the absence of cAMP, may be involved in the pregenomic RNA (pgRNA) encapsidation and DNA-replication in HBV-infected cells.Entities:
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Year: 2006 PMID： 16430890 DOI： 10.1016/j.febslet.2006.01.011
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124