The carboxy terminal domain of RNA polymerase II and alternative splicing
Alternative splicing is controlled by cis-regulatory sequences present in the pre-mRNA and their cognate trans-acting factors, as well as by its coupling to RNA polymerase II (pol II) transcription. A unique feature of this polymerase is the presence of a highly repetitive carboxy terminal domain (C...
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09680004_v35_n9_p497_Munoz http://hdl.handle.net/20.500.12110/paper_09680004_v35_n9_p497_Munoz |
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paper:paper_09680004_v35_n9_p497_Munoz2023-06-08T15:58:49Z The carboxy terminal domain of RNA polymerase II and alternative splicing Muñoz, Manuel Javier de la Mata, Manuel Kornblihtt, Alberto Rodolfo cyclin dependent kinase 7 RNA polymerase II small nuclear ribonucleoprotein alternative RNA splicing carboxy terminal sequence chromatin assembly and disassembly consensus sequence molecular dynamics nonhuman priority journal protein phosphorylation protein processing protein protein interaction review RNA capping RNA processing RNA translation spliceosome transcription regulation Alternative Splicing Animals Humans Phosphorylation Protein Processing, Post-Translational RNA Polymerase II Alternative splicing is controlled by cis-regulatory sequences present in the pre-mRNA and their cognate trans-acting factors, as well as by its coupling to RNA polymerase II (pol II) transcription. A unique feature of this polymerase is the presence of a highly repetitive carboxy terminal domain (CTD), which is subject to multiple regulatory post-translational modifications. CTD phosphorylation events affect the transcriptional properties of pol II and the outcome of co-transcriptional alternative splicing by mediating the effects of splicing factors and by modulating transcription elongation rates. Here, we discuss various examples of involvement of the CTD in alternative splicing regulation as well as the current methodological limitations in deciphering the detailed mechanisms of this process. © 2010 Elsevier Ltd. Fil:Muñoz, M.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:de la Mata, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Kornblihtt, A.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2010 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09680004_v35_n9_p497_Munoz http://hdl.handle.net/20.500.12110/paper_09680004_v35_n9_p497_Munoz |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
cyclin dependent kinase 7 RNA polymerase II small nuclear ribonucleoprotein alternative RNA splicing carboxy terminal sequence chromatin assembly and disassembly consensus sequence molecular dynamics nonhuman priority journal protein phosphorylation protein processing protein protein interaction review RNA capping RNA processing RNA translation spliceosome transcription regulation Alternative Splicing Animals Humans Phosphorylation Protein Processing, Post-Translational RNA Polymerase II |
spellingShingle |
cyclin dependent kinase 7 RNA polymerase II small nuclear ribonucleoprotein alternative RNA splicing carboxy terminal sequence chromatin assembly and disassembly consensus sequence molecular dynamics nonhuman priority journal protein phosphorylation protein processing protein protein interaction review RNA capping RNA processing RNA translation spliceosome transcription regulation Alternative Splicing Animals Humans Phosphorylation Protein Processing, Post-Translational RNA Polymerase II Muñoz, Manuel Javier de la Mata, Manuel Kornblihtt, Alberto Rodolfo The carboxy terminal domain of RNA polymerase II and alternative splicing |
topic_facet |
cyclin dependent kinase 7 RNA polymerase II small nuclear ribonucleoprotein alternative RNA splicing carboxy terminal sequence chromatin assembly and disassembly consensus sequence molecular dynamics nonhuman priority journal protein phosphorylation protein processing protein protein interaction review RNA capping RNA processing RNA translation spliceosome transcription regulation Alternative Splicing Animals Humans Phosphorylation Protein Processing, Post-Translational RNA Polymerase II |
description |
Alternative splicing is controlled by cis-regulatory sequences present in the pre-mRNA and their cognate trans-acting factors, as well as by its coupling to RNA polymerase II (pol II) transcription. A unique feature of this polymerase is the presence of a highly repetitive carboxy terminal domain (CTD), which is subject to multiple regulatory post-translational modifications. CTD phosphorylation events affect the transcriptional properties of pol II and the outcome of co-transcriptional alternative splicing by mediating the effects of splicing factors and by modulating transcription elongation rates. Here, we discuss various examples of involvement of the CTD in alternative splicing regulation as well as the current methodological limitations in deciphering the detailed mechanisms of this process. © 2010 Elsevier Ltd. |
author |
Muñoz, Manuel Javier de la Mata, Manuel Kornblihtt, Alberto Rodolfo |
author_facet |
Muñoz, Manuel Javier de la Mata, Manuel Kornblihtt, Alberto Rodolfo |
author_sort |
Muñoz, Manuel Javier |
title |
The carboxy terminal domain of RNA polymerase II and alternative splicing |
title_short |
The carboxy terminal domain of RNA polymerase II and alternative splicing |
title_full |
The carboxy terminal domain of RNA polymerase II and alternative splicing |
title_fullStr |
The carboxy terminal domain of RNA polymerase II and alternative splicing |
title_full_unstemmed |
The carboxy terminal domain of RNA polymerase II and alternative splicing |
title_sort |
carboxy terminal domain of rna polymerase ii and alternative splicing |
publishDate |
2010 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09680004_v35_n9_p497_Munoz http://hdl.handle.net/20.500.12110/paper_09680004_v35_n9_p497_Munoz |
work_keys_str_mv |
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1768545426893438976 |