TY - JOUR
T1 - Epstein-Barr virus-encoded protein kinase BGLF-4 mediates hyperphosphorylation of cellular elongation factor 1δ (EF-1δ)
T2 - EF-1δ is universally modified by conserved protein kinases of herpesviruses in mammalian cells
AU - Kato, K.
AU - Kawaguchi, Y.
AU - Tanaka, M.
AU - Igarashi, M.
AU - Yokoyama, A.
AU - Matsuda, G.
AU - Kanamori, M.
AU - Nakajima, K.
AU - Nishimura, Y.
AU - Shimojima, M.
AU - Phung, H. T.T.
AU - Takahashi, E.
AU - Hirai, K.
PY - 2001
Y1 - 2001
N2 - Translation elongation factor 1δ (EF-1δ) is hyperphosphorylated in various mammalian cells infected with alpha-, beta- and gammaherpesviruses and EF-1δ 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 [γ-32P]ATP and labelling was eliminated by phosphatase. (ii) The ratio of the hyperphosphorylated form of human EF-1δ 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-1δ hyperphosphorylation. These data also support the hypothesis that the protein kinases that are conserved by herpesviruses universally mediate EF-1δ modification in mammalian cells.
AB - Translation elongation factor 1δ (EF-1δ) is hyperphosphorylated in various mammalian cells infected with alpha-, beta- and gammaherpesviruses and EF-1δ 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 [γ-32P]ATP and labelling was eliminated by phosphatase. (ii) The ratio of the hyperphosphorylated form of human EF-1δ 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-1δ hyperphosphorylation. These data also support the hypothesis that the protein kinases that are conserved by herpesviruses universally mediate EF-1δ modification in mammalian cells.
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U2 - 10.1099/0022-1317-82-6-1457
DO - 10.1099/0022-1317-82-6-1457
M3 - Article
C2 - 11369891
AN - SCOPUS:17144468445
VL - 82
SP - 1457
EP - 1463
JO - Journal of General Virology
JF - Journal of General Virology
SN - 0022-1317
IS - 6
ER -