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PIAS1 enhances SUMO‐1 modification and the transactivation activity of the major immediate–early IE2 protein of human cytomegalovirus
Author(s) -
Lee Jang-Mi,
Kang Hee-Jung,
Lee Hye-Ra,
Choi Cheol Yong,
Jang Won-Jong,
Ahn Jin-Hyun
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01268-7
Subject(s) - transactivation , human cytomegalovirus , chemistry , cytomegalovirus , virology , biology , biochemistry , virus , gene , herpesviridae , gene expression , viral disease
The protein inhibitor of activated STAT1 (PIAS1), known to be a small ubiquitin‐like modifier (SUMO) E3 ligase, was found to interact with the human cytomegalovirus IE2 protein. We found that the sumoylation of IE2 was markedly enhanced by wild‐type PIAS1 but not by a mutant containing a Cys to Ser substitution at position 351 (C351S) within the RING finger‐like domain. In target reporter gene assays, wild‐type PIAS1, but not the C351S mutant, enhanced the IE2‐mediated transactivations of viral polymerase promoter and cellular cyclin E promoter and this augmentation required the intact sumoylation sites of IE2. Our results suggest that PIAS1 acts as a SUMO E3 ligase toward IE2 and that it may regulate the transactivation function of IE2. To our knowledge, IE2 is the first viral target found to be regulated by a SUMO E3 ligase.