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PMID: 7559785 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies.

The Journal of cell biology ·Vol. 131 ·No. 1 ·1995-10-00 ·Pages 45-56

Carvalho T, Seeler JS, Ohman K, Jordan P, Pettersson U, Akusjärvi G, Carmo-Fonseca M, Dejean A

Abstract

The PML protein was first identified as part of a fusion product with the retinoic acid receptor alpha (RAR alpha), resulting from the t(15;17) chromosomal translocation associated with acute promyelocytic leukemia (APL). It has been previously demonstrated that PML, which is tightly bound to the nuclear matrix, concentrates in discrete subnuclear compartments that are disorganized in APL cells due to the expression of the PML-RAR alpha hybrid. Here we report that adenovirus infection causes a drastic redistribution of PML from spherical nuclear bodies into fibrous structures. The product encoded by adenovirus E4-ORF3 is shown to be responsible for this reorganization and to colocalize with PML into these fibers. In addition, we demonstrate that E1A oncoproteins concentrate in the PML domains, both in infected and transiently transfected cells, and that this association requires the conserved amino acid motif (D)LXCXE, common to all viral oncoproteins that bind pRB or the related p107 and p130 proteins. The SV-40 large T antigen, another member of this oncoprotein family is also found in close association with the PML nuclear bodies. Taken together, the present data indicate that the subnuclear domains containing PML represent a preferential target for DNA tumor viruses, and therefore suggest a more general involvement of the PML nuclear bodies in oncogenic processes.

MeSH Terms
Adenovirus E1A Proteins/metabolism Adenovirus E4 Proteins/metabolism Amino Acid Sequence Antigens, Polyomavirus Transforming/metabolism Bacterial Adhesion Bacterial Proteins HeLa Cells/metabolism,ultrastructure,virology Humans Microscopy, Electron Molecular Sequence Data Neoplasm Proteins Nuclear Matrix/metabolism Nuclear Proteins Oncogene Proteins/metabolism Open Reading Frames Promyelocytic Leukemia Protein Transcription Factors/metabolism Tumor Suppressor Proteins
Chemicals
Adenovirus E1A Proteins Adenovirus E4 Proteins Antigens, Polyomavirus Transforming Bacterial Proteins Neoplasm Proteins Nuclear Proteins Oncogene Proteins Promyelocytic Leukemia Protein Transcription Factors Tumor Suppressor Proteins PML protein, human
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Carvalho T
Instituto de Histologia, Faculdade de Medicina, Lisboa, Portugal.
Seeler J S
Ohman K
Jordan P
Pettersson U
Akusjärvi G
Carmo-Fonseca M
Dejean A
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
1995-10-00
Pages
45-56
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2120608
Subset
IM
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