High phosphorylation of HBV core protein by two alpha-type CK2-activated cAMP-dependent protein kinases in vitro.

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 Lett

journal_title

FEBS letters

authors

Enomoto M,Sawano Y,Kosuge S,Yamano Y,Kuroki K,Ohtsuki K

doi

10.1016/j.febslet.2006.01.011

keywords:

subject

Has Abstract

pub_date

2006-02-06 00:00:00

pages

894-9

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)00044-5

journal_volume

580

pub_type

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