PMID- 11901159
OWN - NLM
STAT- MEDLINE
DCOM- 20020702
LR  - 20210206
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 277
IP  - 22
DP  - 2002 May 31
TI  - Human Herpesvirus 6 immediate-early 1 protein is a sumoylated nuclear 
      phosphoprotein colocalizing with promyelocytic leukemia protein-associated 
      nuclear bodies.
PG  - 19679-87
AB  - Immediate-early (IE) proteins are the first proteins expressed following viral 
      entry and play a crucial role in the initiation of infection. We report the 
      cloning and characterization of a full-length IE1 transcript and protein (IE1B) 
      from human herpesvirus 6 (HHV-6) variant B. The IE1B transcript consists of five 
      exons (3720 nucleotides), three of which are coding for the IE1 protein. The 
      1078-amino acid-long IE1B protein is 62% identical and 75% similar to the 
      941-amino acid IE1 from HHV-6 variant A. IE1B protein can be detected at 4 h 
      post-infection (P.I.), and it is distributed as small intranuclear structures. 
      The maximal number of IE1 bodies ( approximately 10-12/nucleus) is detected at 12 
      h P.I. after which the IE1 bodies condense into 1-3 larger entities by 24-48 h 
      P.I. During infection the IE1B protein is phosphorylated on serine and threonine 
      residues. IE1B undergoes further post-translational modification with its 
      conjugation to the small ubiquitin-like modifier (SUMO-1) peptide. IE1B 
      colocalizes with SUMO-1 and promyelocytic leukemia nuclear bodies during 
      infection as well as in transfection experiments. Finally, IE1 from variant B is 
      a weaker transactivator than IE1 from variant A, when assayed using heterologous 
      promoters. Overall, the characterization of the HHV-6 IE1B protein presented 
      highlights the similarity and divergence between IE1 from both variants and 
      provides useful information pertaining to the early phase of infection.
FAU - Gravel, Annie
AU  - Gravel A
AD  - Laboratory of Virology, Laboratory of Viral Immunology, Rheumatology and 
      Immunology Research Center, Centre Hospitalier de l'Universite Laval Research 
      Center and Faculty of Medicine, Laval University, Sainte-Foy, Quebec G1V 4G2, 
      Canada.
FAU - Gosselin, Jean
AU  - Gosselin J
FAU - Flamand, Louis
AU  - Flamand L
LA  - eng
SI  - GENBANK/AY037932
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20020318
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - 0 (Immediate-Early Proteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (Promyelocytic Leukemia Protein)
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Transcription Factors)
RN  - 0 (Tumor Suppressor Proteins)
RN  - 0 (immediate-early 1 protein, human herpesvirus 6)
RN  - 143220-95-5 (PML protein, human)
RN  - 2ZD004190S (Threonine)
RN  - 452VLY9402 (Serine)
RN  - 63231-63-0 (RNA)
RN  - EC 2.5.1.18 (Glutathione Transferase)
SB  - IM
MH  - Cell Nucleus/*metabolism
MH  - Cell-Free System
MH  - Cloning, Molecular
MH  - DNA, Complementary/metabolism
MH  - Exons
MH  - Genetic Vectors
MH  - Glutathione Transferase/metabolism
MH  - Herpesvirus 6, Human/*metabolism
MH  - Humans
MH  - Immediate-Early Proteins/*chemistry/*metabolism
MH  - Kinetics
MH  - Models, Genetic
MH  - Molecular Sequence Data
MH  - Neoplasm Proteins/*metabolism
MH  - *Nuclear Proteins
MH  - Phosphoproteins/*chemistry/*metabolism
MH  - Phosphorylation
MH  - Promoter Regions, Genetic
MH  - Promyelocytic Leukemia Protein
MH  - Protein Binding
MH  - Protein Biosynthesis
MH  - Protein Processing, Post-Translational
MH  - RNA/metabolism
MH  - RNA, Messenger/metabolism
MH  - Recombinant Fusion Proteins/metabolism
MH  - Serine/chemistry
MH  - Spectrometry, Fluorescence
MH  - Threonine/chemistry
MH  - Time Factors
MH  - Transcription Factors/*metabolism
MH  - Transcription, Genetic
MH  - Transfection
MH  - Tumor Cells, Cultured
MH  - Tumor Suppressor Proteins
EDAT- 2002/03/20 10:00
MHDA- 2002/07/03 10:01
CRDT- 2002/03/20 10:00
PHST- 2002/03/20 10:00 [pubmed]
PHST- 2002/07/03 10:01 [medline]
PHST- 2002/03/20 10:00 [entrez]
AID - S0021-9258(20)85032-7 [pii]
AID - 10.1074/jbc.M200836200 [doi]
PST - ppublish
SO  - J Biol Chem. 2002 May 31;277(22):19679-87. doi: 10.1074/jbc.M200836200. Epub 2002 
      Mar 18.