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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Enomoto M,Sawano Y,Kosuge S,Yamano Y,Kuroki K,Ohtsuki Kdoi
10.1016/j.febslet.2006.01.011keywords:
subject
Has Abstractpub_date
2006-02-06 00:00:00pages
894-9issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(06)00044-5journal_volume
580pub_type
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