| Literature DB >> 11369891 |
Kentaro Kato1,2, Yasushi Kawaguchi2, Michiko Tanaka2, Mie Igarashi2, Akihiko Yokoyama2, Go Matsuda2, Mikiko Kanamori2, Kaori Nakajima2, Yorihiro Nishimura1, Masayuki Shimojima1, Hang T T Phung1, Eiji Takahashi1, Kanji Hirai2.
Abstract
Translation elongation factor 1delta (EF-1delta) is hyperphosphorylated in various mammalian cells infected with alpha-, beta- and gammaherpesviruses and EF-1delta modification is mediated by viral protein kinases, including UL13 of herpes simplex virus type 1 and UL97 of human cytomegalovirus. In this study, the following is reported. (i) BGLF4 encoded by the prototype gammaherpesvirus Epstein-Barr virus was purified as a fusion protein that was labelled with [gamma-(32)P]ATP and labelling was eliminated by phosphatase. (ii) The ratio of the hyperphosphorylated form of human EF-1delta was increased both in Sf9 cells after infection with baculoviruses expressing GST-BGLF4 fusion proteins and in COS-7 cells after transfection with a BGLF4 expression plasmid. These results indicate that purified BGLF4 possesses protein kinase activity and mediates EF-1delta hyperphosphorylation. These data also support the hypothesis that the protein kinases that are conserved by herpesviruses universally mediate EF-1delta modification in mammalian cells.Entities:
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Year: 2001 PMID: 11369891 DOI: 10.1099/0022-1317-82-6-1457
Source DB: PubMed Journal: J Gen Virol ISSN: 0022-1317 Impact factor: 3.891