1 anslation factor, elongation factor delta-1 (EF-1delta).

2    The translation elongation factor 1delta (EF-1delta) consists of two forms, a hypophosphorylated f

3 ence identity with elongation factor-1delta (EF-1delta), a member of the multimeric complex regulatin

4 east EF-1beta, even though both EF-1beta and EF-1delta have previously been shown to have guanine nuc

5                Human EF-1beta, but not human EF-1delta, is functional in place of yeast EF-1beta, eve

6 ive amounts of hypo- and hyperphosphorylated EF-1delta in Vero cells infected with mutant virus lacki

7 erential accumulation of hyperphosphorylated EF-1delta was observed in cells infected with viruses fr

8  (ii) The absence of the hyperphosphorylated EF-1delta in cells infected with the U(L)13 deletion mut

9  the accumulation of the hyperphosphorylated EF-1delta is due to phosphorylation by U(L)13 protein ki

10 ut the prevalence of the hyperphosphorylated EF-1delta was dependent on the presence of the U(L)13 pr

11         In contrast, the hyperphosphorylated EF-1delta was the predominant form in Vero cells infecte

12                                         (iv) EF-1delta immunoprecipitated from uninfected Vero cells

13                 (v) The predominant forms of EF-1delta on electrophoresis in denaturing gels have app

14                          (iii) Both forms of EF-1delta were labeled by 32Pi in vivo, but the prevalen

15 1beta and the metazoan EF-1beta-like protein EF-1delta is highly conserved.

16  of glutathione S-transferase (GST) fused to EF-1delta specifically formed complexes with ICP0 contai

17  with evidence that ICP0 also interacts with EF-1delta reported in the paper cited above, these data