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HIV-1 Tat interacts with LIS1 protein
BACKGROUND: HIV-1 Tat activates transcription of HIV-1 viral genes by inducing phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (RNAPII). Tat can also disturb cellular metabolism by inhibiting proliferation of antigen-specific T lymphocytes and by inducing cellular apoptosis. Tat-...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2005
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC549217/ https://www.ncbi.nlm.nih.gov/pubmed/15698475 http://dx.doi.org/10.1186/1742-4690-2-6 |
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author | Epie, Nicolas Ammosova, Tatyana Sapir, Tamar Voloshin, Yaroslav Lane, William S Turner, Willie Reiner, Orly Nekhai, Sergei |
author_facet | Epie, Nicolas Ammosova, Tatyana Sapir, Tamar Voloshin, Yaroslav Lane, William S Turner, Willie Reiner, Orly Nekhai, Sergei |
author_sort | Epie, Nicolas |
collection | PubMed |
description | BACKGROUND: HIV-1 Tat activates transcription of HIV-1 viral genes by inducing phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (RNAPII). Tat can also disturb cellular metabolism by inhibiting proliferation of antigen-specific T lymphocytes and by inducing cellular apoptosis. Tat-induced apoptosis of T-cells is attributed, in part, to the distortion of microtubules polymerization. LIS1 is a microtubule-associated protein that facilitates microtubule polymerization. RESULTS: We identified here LIS1 as a Tat-interacting protein during extensive biochemical fractionation of T-cell extracts. We found several proteins to co-purify with a Tat-associated RNAPII CTD kinase activity including LIS1, CDK7, cyclin H, and MAT1. Tat interacted with LIS1 but not with CDK7, cyclin H or MAT1 in vitro. LIS1 also co-immunoprecipitated with Tat expressed in HeLa cells. Further, LIS1 interacted with Tat in a yeast two-hybrid system. CONCLUSION: Our results indicate that Tat interacts with LIS1 in vitro and in vivo and that this interaction might contribute to the effect of Tat on microtubule formation. |
format | Text |
id | pubmed-549217 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-5492172005-02-23 HIV-1 Tat interacts with LIS1 protein Epie, Nicolas Ammosova, Tatyana Sapir, Tamar Voloshin, Yaroslav Lane, William S Turner, Willie Reiner, Orly Nekhai, Sergei Retrovirology Research BACKGROUND: HIV-1 Tat activates transcription of HIV-1 viral genes by inducing phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (RNAPII). Tat can also disturb cellular metabolism by inhibiting proliferation of antigen-specific T lymphocytes and by inducing cellular apoptosis. Tat-induced apoptosis of T-cells is attributed, in part, to the distortion of microtubules polymerization. LIS1 is a microtubule-associated protein that facilitates microtubule polymerization. RESULTS: We identified here LIS1 as a Tat-interacting protein during extensive biochemical fractionation of T-cell extracts. We found several proteins to co-purify with a Tat-associated RNAPII CTD kinase activity including LIS1, CDK7, cyclin H, and MAT1. Tat interacted with LIS1 but not with CDK7, cyclin H or MAT1 in vitro. LIS1 also co-immunoprecipitated with Tat expressed in HeLa cells. Further, LIS1 interacted with Tat in a yeast two-hybrid system. CONCLUSION: Our results indicate that Tat interacts with LIS1 in vitro and in vivo and that this interaction might contribute to the effect of Tat on microtubule formation. BioMed Central 2005-02-07 /pmc/articles/PMC549217/ /pubmed/15698475 http://dx.doi.org/10.1186/1742-4690-2-6 Text en Copyright © 2005 Epie et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Epie, Nicolas Ammosova, Tatyana Sapir, Tamar Voloshin, Yaroslav Lane, William S Turner, Willie Reiner, Orly Nekhai, Sergei HIV-1 Tat interacts with LIS1 protein |
title | HIV-1 Tat interacts with LIS1 protein |
title_full | HIV-1 Tat interacts with LIS1 protein |
title_fullStr | HIV-1 Tat interacts with LIS1 protein |
title_full_unstemmed | HIV-1 Tat interacts with LIS1 protein |
title_short | HIV-1 Tat interacts with LIS1 protein |
title_sort | hiv-1 tat interacts with lis1 protein |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC549217/ https://www.ncbi.nlm.nih.gov/pubmed/15698475 http://dx.doi.org/10.1186/1742-4690-2-6 |
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