PIAS1 enhances SUMO-1 modification and the transactivation activity of the major immediate–early IE2 protein of human cytomegalovirus

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...

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Bibliographic Details
Published in:FEBS letters 2003-12, Vol.555 (2), p.322-328
Main Authors: Lee, Jang-Mi, Kang, Hee-Jung, Lee, Hye-Ra, Choi, Cheol Yong, Jang, Won-Jong, Ahn, Jin-Hyun
Format: Article
Language:English
Subjects:
Amino Acid Substitution
Animals
Binding Sites
Cell Line
Cytomegalovirus - genetics
Cytomegalovirus - metabolism
DNA-Directed DNA Polymerase - genetics
DNA-Directed DNA Polymerase - metabolism
Galactosidases - metabolism
Genes, Reporter - genetics
Human cytomegalovirus
Humans
Immediate-Early Proteins - genetics
Immediate-Early Proteins - metabolism
Immediate–early protein
Promoter Regions, Genetic
Protein inhibitor of activated STAT1
Protein Inhibitors of Activated STAT
Protein Structure, Tertiary
Proteins - chemistry
Proteins - genetics
Proteins - metabolism
Proteins - pharmacology
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Recombinant Fusion Proteins - pharmacology
Small ubiquitin-like modifier-1
SUMO-1 Protein - metabolism
Trans-Activators - metabolism
Transcriptional Activation
Transfection
Ubiquitin-Protein Ligases - metabolism
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(03)01268-7