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The elongation factor Spn1 is a multi-functional chromatin binding protein
The process of transcriptional elongation by RNA polymerase II (RNAPII) in a chromatin context involves a large number of crucial factors. Spn1 is a highly conserved protein encoded by an essential gene and is known to interact with RNAPII and the histone chaperone Spt6. Spn1 negatively regulates th...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5861400/ https://www.ncbi.nlm.nih.gov/pubmed/29300974 http://dx.doi.org/10.1093/nar/gkx1305 |
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author | Li, Sha Almeida, Adam R Radebaugh, Catherine A Zhang, Ling Chen, Xu Huang, Liangqun Thurston, Alison K Kalashnikova, Anna A Hansen, Jeffrey C Luger, Karolin Stargell, Laurie A |
author_facet | Li, Sha Almeida, Adam R Radebaugh, Catherine A Zhang, Ling Chen, Xu Huang, Liangqun Thurston, Alison K Kalashnikova, Anna A Hansen, Jeffrey C Luger, Karolin Stargell, Laurie A |
author_sort | Li, Sha |
collection | PubMed |
description | The process of transcriptional elongation by RNA polymerase II (RNAPII) in a chromatin context involves a large number of crucial factors. Spn1 is a highly conserved protein encoded by an essential gene and is known to interact with RNAPII and the histone chaperone Spt6. Spn1 negatively regulates the ability of Spt6 to interact with nucleosomes, but the chromatin binding properties of Spn1 are largely unknown. Here, we demonstrate that full length Spn1 (amino acids 1–410) binds DNA, histones H3–H4, mononucleosomes and nucleosomal arrays, and has weak nucleosome assembly activity. The core domain of Spn1 (amino acids 141–305), which is necessary and sufficient in Saccharomyces cerevisiae for growth under ideal growth conditions, is unable to optimally interact with histones, nucleosomes and/or DNA and fails to assemble nucleosomes in vitro. Although competent for binding with Spt6 and RNAPII, the core domain derivative is not stably recruited to the CYC1 promoter, indicating chromatin interactions are an important aspect of normal Spn1 functions in vivo. Moreover, strong synthetic genetic interactions are observed with Spn1 mutants and deletions of histone chaperone genes. Taken together, these results indicate that Spn1 is a histone binding factor with histone chaperone functions. |
format | Online Article Text |
id | pubmed-5861400 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-58614002018-03-28 The elongation factor Spn1 is a multi-functional chromatin binding protein Li, Sha Almeida, Adam R Radebaugh, Catherine A Zhang, Ling Chen, Xu Huang, Liangqun Thurston, Alison K Kalashnikova, Anna A Hansen, Jeffrey C Luger, Karolin Stargell, Laurie A Nucleic Acids Res Gene regulation, Chromatin and Epigenetics The process of transcriptional elongation by RNA polymerase II (RNAPII) in a chromatin context involves a large number of crucial factors. Spn1 is a highly conserved protein encoded by an essential gene and is known to interact with RNAPII and the histone chaperone Spt6. Spn1 negatively regulates the ability of Spt6 to interact with nucleosomes, but the chromatin binding properties of Spn1 are largely unknown. Here, we demonstrate that full length Spn1 (amino acids 1–410) binds DNA, histones H3–H4, mononucleosomes and nucleosomal arrays, and has weak nucleosome assembly activity. The core domain of Spn1 (amino acids 141–305), which is necessary and sufficient in Saccharomyces cerevisiae for growth under ideal growth conditions, is unable to optimally interact with histones, nucleosomes and/or DNA and fails to assemble nucleosomes in vitro. Although competent for binding with Spt6 and RNAPII, the core domain derivative is not stably recruited to the CYC1 promoter, indicating chromatin interactions are an important aspect of normal Spn1 functions in vivo. Moreover, strong synthetic genetic interactions are observed with Spn1 mutants and deletions of histone chaperone genes. Taken together, these results indicate that Spn1 is a histone binding factor with histone chaperone functions. Oxford University Press 2018-03-16 2017-12-30 /pmc/articles/PMC5861400/ /pubmed/29300974 http://dx.doi.org/10.1093/nar/gkx1305 Text en © The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Gene regulation, Chromatin and Epigenetics Li, Sha Almeida, Adam R Radebaugh, Catherine A Zhang, Ling Chen, Xu Huang, Liangqun Thurston, Alison K Kalashnikova, Anna A Hansen, Jeffrey C Luger, Karolin Stargell, Laurie A The elongation factor Spn1 is a multi-functional chromatin binding protein |
title | The elongation factor Spn1 is a multi-functional chromatin binding protein |
title_full | The elongation factor Spn1 is a multi-functional chromatin binding protein |
title_fullStr | The elongation factor Spn1 is a multi-functional chromatin binding protein |
title_full_unstemmed | The elongation factor Spn1 is a multi-functional chromatin binding protein |
title_short | The elongation factor Spn1 is a multi-functional chromatin binding protein |
title_sort | elongation factor spn1 is a multi-functional chromatin binding protein |
topic | Gene regulation, Chromatin and Epigenetics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5861400/ https://www.ncbi.nlm.nih.gov/pubmed/29300974 http://dx.doi.org/10.1093/nar/gkx1305 |
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