THE UL13 GENE OF HERPES-SIMPLEX VIRUS-1 ENCODES THE FUNCTIONS FOR POSTTRANSLATIONAL PROCESSING ASSOCIATED WITH PHOSPHORYLATION OF THE REGULATORY PROTEIN-ALPHA-22
THE UL13 GENE OF HERPES-SIMPLEX VIRUS-1 ENCODES THE FUNCTIONS FOR POSTTRANSLATIONAL PROCESSING ASSOCIATED WITH PHOSPHORYLATION OF THE REGULATORY PROTEIN-ALPHA-22
复制标题
DOI:
10.1073/pnas.89.16.7310
复制
发表时间:
1992-08-15
影响因子:
11.1
通讯作者:
ROIZMAN, B
中科院分区:
文献类型:
--
作者:
PURVES, FC;ROIZMAN, B
The herpes simplex virus 1 genome was shown to encode two genes, U(S)3 and U(L)13, exhibiting amino acid sequence motifs common to protein kinases. Elsewhere this laboratory reported that the prominent substrate of the U(S)3 protein kinase is the product of the U(L)34 gene, an essential nonglycosylated membrane protein. In the absence of the U(S)3 kinase, the U(L)34 protein remains unphosphorylated but forms a complex with four proteins that become phosphorylated uniquely when U(L)34 is not. To investigate the role of U(L)13 protein in this process, recombinant viruses lacking U(L)13 or both U(L)13 and U(S)3 were constructed. We report that U(L)13 is dispensable for viral replication in cell culture and is not involved in the processing of U(L)34 or of associated phosphoproteins. U(L)13 is, however, responsible for the posttranslational processing associated with phosphorylation of infected-cell protein 22, the product of the alpha-22 gene. This gene was previously reported to play a regulatory role in selected cell lines. U(L)13 appears to be either a protein kinase or a phosphotransferase and its major substrate is the alpha-22 protein.