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Extension of the minimal functional unit of the RNA polymerase II CTD from yeast to mammalian cells

The carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) consists of 26 and 52 heptad-repeats in yeast and mammals, respectively. Studies in yeast showed that the strong periodicity of the YSPTSPS heptads is dispensable for cell growth and that di-heptads interspersed b...

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Autores principales: Shah, Nilay, Decker, Tim-Michael, Eick, Dirk
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6548728/
https://www.ncbi.nlm.nih.gov/pubmed/31088280
http://dx.doi.org/10.1098/rsbl.2019.0068
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author Shah, Nilay
Decker, Tim-Michael
Eick, Dirk
author_facet Shah, Nilay
Decker, Tim-Michael
Eick, Dirk
author_sort Shah, Nilay
collection PubMed
description The carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) consists of 26 and 52 heptad-repeats in yeast and mammals, respectively. Studies in yeast showed that the strong periodicity of the YSPTSPS heptads is dispensable for cell growth and that di-heptads interspersed by spacers can act as minimal functional units (MFUs) to fulfil all essential CTD functions. Here, we show that the MFU of mammalian cells is significantly larger than in yeast and consists of penta-heptads. We further show that the distance between two MFUs is critical for the functions of mammalian CTD. Our study suggests that the general structure of the CTD remained largely unchanged in yeast and mammals; however, besides the number of heptad-repeats, also the length of the MFU significantly increased in mammals.
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spelling pubmed-65487282019-06-12 Extension of the minimal functional unit of the RNA polymerase II CTD from yeast to mammalian cells Shah, Nilay Decker, Tim-Michael Eick, Dirk Biol Lett Molecular Evolution The carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) consists of 26 and 52 heptad-repeats in yeast and mammals, respectively. Studies in yeast showed that the strong periodicity of the YSPTSPS heptads is dispensable for cell growth and that di-heptads interspersed by spacers can act as minimal functional units (MFUs) to fulfil all essential CTD functions. Here, we show that the MFU of mammalian cells is significantly larger than in yeast and consists of penta-heptads. We further show that the distance between two MFUs is critical for the functions of mammalian CTD. Our study suggests that the general structure of the CTD remained largely unchanged in yeast and mammals; however, besides the number of heptad-repeats, also the length of the MFU significantly increased in mammals. The Royal Society 2019-05 2019-05-15 /pmc/articles/PMC6548728/ /pubmed/31088280 http://dx.doi.org/10.1098/rsbl.2019.0068 Text en © 2019 The Authors. http://creativecommons.org/licenses/by/4.0/ Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.
spellingShingle Molecular Evolution
Shah, Nilay
Decker, Tim-Michael
Eick, Dirk
Extension of the minimal functional unit of the RNA polymerase II CTD from yeast to mammalian cells
title Extension of the minimal functional unit of the RNA polymerase II CTD from yeast to mammalian cells
title_full Extension of the minimal functional unit of the RNA polymerase II CTD from yeast to mammalian cells
title_fullStr Extension of the minimal functional unit of the RNA polymerase II CTD from yeast to mammalian cells
title_full_unstemmed Extension of the minimal functional unit of the RNA polymerase II CTD from yeast to mammalian cells
title_short Extension of the minimal functional unit of the RNA polymerase II CTD from yeast to mammalian cells
title_sort extension of the minimal functional unit of the rna polymerase ii ctd from yeast to mammalian cells
topic Molecular Evolution
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6548728/
https://www.ncbi.nlm.nih.gov/pubmed/31088280
http://dx.doi.org/10.1098/rsbl.2019.0068
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