PMID- 15105549
OWN - NLM
STAT- MEDLINE
DCOM- 20040614
LR  - 20200303
IS  - 0022-1317 (Print)
IS  - 0022-1317 (Linking)
VI  - 85
IP  - Pt 5
DP  - 2004 May
TI  - Characterization of human herpesvirus 6 variant B immediate-early 1 protein 
      modifications by small ubiquitin-related modifiers.
PG  - 1319-1328
LID - 10.1099/vir.0.19610-0 [doi]
AB  - The human herpesvirus 6 (HHV-6) immediate-early (IE) 1 protein undergoes 
      SUMOylation events during the infectious process. In the present work, we report 
      that Lys-802 (K-802) of IE1 from HHV-6 variant B is the only target residue 
      capable of conjugation to SUMO-1/SMT3C/Sentrin-1, SUMO-2/SMT3A/Sentrin-3 or 
      SUMO-3/SMT3B/Sentrin-2 as determined by transfection and in vitro SUMOylation 
      experiments. PolySUMOylated forms of IE1 were also observed, suggesting that SUMO 
      branching occurs at the K-802 residue. Overexpression of SUMO-1, -2 and -3 led to 
      an overall increase in IE1 levels, irrespective of K-802. The SUMO residues could 
      be efficiently removed by incubating SUMOylated IE1 with SENP1, a recently 
      identified SUMO peptidase. SUMOylation-deficient mutants of IE1 co-localized with 
      nuclear promyelocytic leukaemia protein (PML) oncogenic domains (PODs) as 
      efficiently as WT IE1, indicating that POD targeting is independent of IE1 
      SUMOylation status. However, in contrast to infection, PODs did not aggregate in 
      IE1B-transfected cells, suggesting that other viral proteins are involved in the 
      process. Transactivation studies indicated that IE1, in combination with IE2, 
      could efficiently transactivate diverse promoters, independent of its SUMOylation 
      status. Overall, the results presented provide a detailed biochemical 
      characterization of post-translational modifications of the HHV-6 IE1 protein by 
      SUMO peptides, contributing to our understanding of the complex interactions 
      between herpesviruses and the SUMO-conjugation pathway.
FAU - Gravel, Annie
AU  - Gravel A
AD  - Laboratory of Virology, Rheumatology and Immunology Research Center, Room T1-49, 
      CHUL Research Center and Faculty of Medicine, Laval University, 2705 Laurier 
      Blvd, Sainte-Foy, Quebec, Canada G1V 4G2.
FAU - Dion, Valerie
AU  - Dion V
AD  - Laboratory of Virology, Rheumatology and Immunology Research Center, Room T1-49, 
      CHUL Research Center and Faculty of Medicine, Laval University, 2705 Laurier 
      Blvd, Sainte-Foy, Quebec, Canada G1V 4G2.
FAU - Cloutier, Nathalie
AU  - Cloutier N
AD  - Laboratory of Virology, Rheumatology and Immunology Research Center, Room T1-49, 
      CHUL Research Center and Faculty of Medicine, Laval University, 2705 Laurier 
      Blvd, Sainte-Foy, Quebec, Canada G1V 4G2.
FAU - Gosselin, Jean
AU  - Gosselin J
AD  - Laboratory of Viral Immunology, Rheumatology and Immunology Research Center, Room 
      T1-49, CHUL Research Center and Faculty of Medicine, Laval University, 2705 
      Laurier Blvd, Sainte-Foy, Quebec, Canada G1V 4G2.
FAU - Flamand, Louis
AU  - Flamand L
AD  - Laboratory of Virology, Rheumatology and Immunology Research Center, Room T1-49, 
      CHUL Research Center and Faculty of Medicine, Laval University, 2705 Laurier 
      Blvd, Sainte-Foy, Quebec, Canada G1V 4G2.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Gen Virol
JT  - The Journal of general virology
JID - 0077340
RN  - 0 (Immediate-Early Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (Small Ubiquitin-Related Modifier Proteins)
RN  - 0 (immediate-early 1 protein, human herpesvirus 6)
RN  - K3Z4F929H6 (Lysine)
SB  - IM
MH  - Animals
MH  - Cell Line
MH  - Herpesvirus 6, Human/*metabolism
MH  - Immediate-Early Proteins/genetics/*metabolism
MH  - Lysine
MH  - Mutation
MH  - Phosphoproteins/genetics/*metabolism
MH  - *Protein Processing, Post-Translational
MH  - Protein Structure, Tertiary
MH  - Small Ubiquitin-Related Modifier Proteins/*metabolism
EDAT- 2004/04/24 05:00
MHDA- 2004/06/15 05:00
CRDT- 2004/04/24 05:00
PHST- 2004/04/24 05:00 [pubmed]
PHST- 2004/06/15 05:00 [medline]
PHST- 2004/04/24 05:00 [entrez]
AID - 10.1099/vir.0.19610-0 [doi]
PST - ppublish
SO  - J Gen Virol. 2004 May;85(Pt 5):1319-1328. doi: 10.1099/vir.0.19610-0.