PMID- 10196275
OWN - NLM
STAT- MEDLINE
DCOM- 19990519
LR  - 20181113
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 73
IP  - 5
DP  - 1999 May
TI  - A novel cellular protein, p60, interacting with both herpes simplex virus 1
      regulatory proteins ICP22 and ICP0 is modified in a cell-type-specific manner and
      Is recruited to the nucleus after infection.
PG  - 3810-7
AB  - Herpes simplex virus 1 encodes two multifunctional regulatory proteins,
      infected-cell proteins 22 and 0 (ICP22 and ICP0). ICP0 is a promiscuous
      transactivator, whereas ICP22 is required in vivo and for efficient replication
      and expression of a subset of late (gamma2) genes in rodent or rabbit cell lines 
      and in primary human cell strains (restrictive cells) but not in HEp-2 or Vero
      (permissive) cells. We report the identification in the yeast two-hybrid system
      of a cellular protein designated p60 that interacts with ICP22. This protein
      (apparent Mr of 60,000) has not been previously described and has no known
      motifs. Analyses of p60 revealed the following. (i) p60 bound fast-migrating,
      underprocessed wild-type ICP22 and ICP22 lacking the carboxyl-terminal 24 amino
      acids but not ICP22 lacking the carboxyl-terminal 40 amino acids, whereas the
      previously identified cellular protein p78 (R. Bruni and B. Roizman, J. Virol.
      72:8525-8531, 1998) bound all forms of ICP22. The interaction of p60 with only
      one isoform of ICP22 supports that hypothesis that each isoform of herpes simplex
      virus proteins performs a specific function that may be different from that of
      other isoforms. (ii) p60 also bound ICP0; the binding of ICP0 was independent of 
      that of ICP22. (iii) p60 localized in uninfected rabbit skin cells in both nuclei
      and cytoplasm. In rabbit skin cells infected with wild-type virus, p60 was
      posttranslationally processed to a higher apparent Mr but was not redistributed. 
      Posttranslational processing required the presence of the genes encoding ICP22
      and UL13 protein kinase. (iv) In uninfected HEp-2 cells, p60 localized primarily 
      in nuclei. Soon after infection with wild-type virus, the p60 localized in
      discrete small nuclear structures with ICP0. Late in infection, both ICP0 and p60
      tended to disperse but p60 did not change in apparent Mr. The localization of p60
      was independent of ICP22, but p60 tended to be more localized in small nuclear
      structures and less dispersed in cells infected with mutants lacking the genes
      encoding the UL13 or US3 protein kinases. The results suggest that
      posttranslational modification of p60 is mediated either by ICP0 (permissive
      cells) or by ICP22 and UL13 protein kinase (restrictive rabbit skin cells) and
      that the restrictive phenotype of rabbit skin cells may be related to the failure
      to process p60 by mutants lacking the genes encoding UL13 or ICP22.
FAU - Bruni, R
AU  - Bruni R
AD  - The Marjorie B. Kovler Viral Oncology Laboratories, The University of Chicago,
      Chicago, Illinois 60637, USA.
FAU - Fineschi, B
AU  - Fineschi B
FAU - Ogle, W O
AU  - Ogle WO
FAU - Roizman, B
AU  - Roizman B
LA  - eng
GR  - CA78766/CA/NCI NIH HHS/United States
GR  - R01 CA078766/CA/NCI NIH HHS/United States
GR  - CA71933/CA/NCI NIH HHS/United States
GR  - CA47451/CA/NCI NIH HHS/United States
GR  - T32 CA009273/CA/NCI NIH HHS/United States
GR  - P01 CA071933/CA/NCI NIH HHS/United States
GR  - R37 CA078766/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Bacterial Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (ICP22 protein, human herpesvirus 1)
RN  - 0 (Immediate-Early Proteins)
RN  - 0 (Lipoproteins)
RN  - 0 (P60 protein, bacteria)
RN  - 0 (Viral Proteins)
RN  - 0 (Viral Regulatory and Accessory Proteins)
RN  - 149058-98-0 (EUS1 protein, Equine herpesvirus 1)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
RN  - EC 2.3.2.27 (Vmw110 protein, Human herpesvirus 1)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.1.- (UL13 protein, Simplexvirus)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (US3 protein, Human herpesvirus 1)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Bacterial Proteins
MH  - Base Sequence
MH  - Biological Transport
MH  - Cell Nucleus/metabolism
MH  - DNA, Complementary
MH  - HeLa Cells
MH  - Herpesvirus 1, Human/*metabolism
MH  - Humans
MH  - Immediate-Early Proteins/*metabolism
MH  - Lipoproteins/metabolism
MH  - Molecular Sequence Data
MH  - Protein Kinases/metabolism
MH  - Protein-Serine-Threonine Kinases/metabolism
MH  - Rabbits
MH  - Tumor Cells, Cultured
MH  - Ubiquitin-Protein Ligases
MH  - *Viral Proteins
MH  - Viral Regulatory and Accessory Proteins
PMC - PMC104158
EDAT- 1999/04/10 00:00
MHDA- 1999/04/10 00:01
CRDT- 1999/04/10 00:00
PHST- 1999/04/10 00:00 [pubmed]
PHST- 1999/04/10 00:01 [medline]
PHST- 1999/04/10 00:00 [entrez]
PST - ppublish
SO  - J Virol. 1999 May;73(5):3810-7.