Journal
JOURNAL OF VIROLOGY
Volume 77, Issue 14, Pages 7720-7727Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.77.14.7720-7727.2003
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Funding
- NEI NIH HHS [R01 EY004096, R37 EY004096, EY 04096] Funding Source: Medline
- NIAID NIH HHS [T32 AI 07245, AI 26077, R56 AI026077, AI 19838, T32 AI007245, R01 AI026077, R01 AI019838] Funding Source: Medline
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The human cytomegalovirus UL97 protein is an unusual protein kinase that is able to autophosphorylate and to phosphorylate certain exogenous substrates, including nucleoside analogs such as ganciclovir. However, no natural substrate of UL97 in infected cells has been identified. We report here that recombinant UL44 protein became radiolabeled when incubated with recombinant UL97 and [P-32]ATP and that both proteins could be coimmunoprecipitated by an antibody that recognizes either protein. Subsequent studies showed that highly purified, recombinant UL97 phosphorylated purified, recombinant UL44. This phosphorylation occurred on serine and threonine residues and was sensitive to inhibition by maribavir and to a mutation that inactivates UL97 catalytic activity. Two-dimensional gel electrophoresis revealed the absence of specific phosphorylated forms of UL44 in immunoprecipitates from lysates of cells infected with a UL97 null mutant virus or with wild-type virus in the presence of maribavir. The results indicate that UL97 is sufficient to phosphorylate UL44 in vitro and is necessary for the normal phosphorylation of UL44 in infected cells. This strongly suggests that UL44 is a natural substrate of UL97.
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