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Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix- associated PML bodies
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 nu...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1995
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120608/ https://www.ncbi.nlm.nih.gov/pubmed/7559785 |
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collection | PubMed |
description | 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. |
format | Text |
id | pubmed-2120608 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1995 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21206082008-05-01 Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix- associated PML bodies J Cell Biol Articles 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. The Rockefeller University Press 1995-10-01 /pmc/articles/PMC2120608/ /pubmed/7559785 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix- associated PML bodies |
title | Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix- associated PML bodies |
title_full | Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix- associated PML bodies |
title_fullStr | Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix- associated PML bodies |
title_full_unstemmed | Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix- associated PML bodies |
title_short | Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix- associated PML bodies |
title_sort | targeting of adenovirus e1a and e4-orf3 proteins to nuclear matrix- associated pml bodies |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120608/ https://www.ncbi.nlm.nih.gov/pubmed/7559785 |