Lysine Methylation Modulates the Interaction of Archaeal Chromatin Protein Cren7 With DNA
Cren7 and Sis7d, two chromatin proteins from Sulfolobus islandicus, undergo extensive methylations at multiple lysine residues to various extents. Whether this highly conserved protein serves an epigenetic role in the regulation of the structure and function of the chromosome remains unclear. In the...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8927968/ https://www.ncbi.nlm.nih.gov/pubmed/35308404 http://dx.doi.org/10.3389/fmicb.2022.837737 |
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author | Ding, Niannian Chen, Yuanyuan Chu, Yindi Zhong, Cheng Huang, Li Zhang, Zhenfeng |
author_facet | Ding, Niannian Chen, Yuanyuan Chu, Yindi Zhong, Cheng Huang, Li Zhang, Zhenfeng |
author_sort | Ding, Niannian |
collection | PubMed |
description | Cren7 and Sis7d, two chromatin proteins from Sulfolobus islandicus, undergo extensive methylations at multiple lysine residues to various extents. Whether this highly conserved protein serves an epigenetic role in the regulation of the structure and function of the chromosome remains unclear. In the present study, we show that methylation significantly affects Cren7, but not Sis7d, in the ability to bind DNA and to constrain negative DNA supercoils. Strikingly, methylated Cren7 was significantly less efficient in forming oligomers or mediating intermolecular DNA bridging. Single-site substitution mutation with glutamine reveals that methylation of the four lysine residues (K24, K31, K42, and K48) of Cren7 at the protein-DNA interface, which are variably conserved among Cren7 homologues from different branches of the Crenarchaeota, influenced Cren7-DNA interactions in different manners. We suggest that dynamic methylation of Cren7 may represent a potential epigenetic mechanism involved in the chromosomal regulation in crenarchaea. |
format | Online Article Text |
id | pubmed-8927968 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-89279682022-03-18 Lysine Methylation Modulates the Interaction of Archaeal Chromatin Protein Cren7 With DNA Ding, Niannian Chen, Yuanyuan Chu, Yindi Zhong, Cheng Huang, Li Zhang, Zhenfeng Front Microbiol Microbiology Cren7 and Sis7d, two chromatin proteins from Sulfolobus islandicus, undergo extensive methylations at multiple lysine residues to various extents. Whether this highly conserved protein serves an epigenetic role in the regulation of the structure and function of the chromosome remains unclear. In the present study, we show that methylation significantly affects Cren7, but not Sis7d, in the ability to bind DNA and to constrain negative DNA supercoils. Strikingly, methylated Cren7 was significantly less efficient in forming oligomers or mediating intermolecular DNA bridging. Single-site substitution mutation with glutamine reveals that methylation of the four lysine residues (K24, K31, K42, and K48) of Cren7 at the protein-DNA interface, which are variably conserved among Cren7 homologues from different branches of the Crenarchaeota, influenced Cren7-DNA interactions in different manners. We suggest that dynamic methylation of Cren7 may represent a potential epigenetic mechanism involved in the chromosomal regulation in crenarchaea. Frontiers Media S.A. 2022-03-03 /pmc/articles/PMC8927968/ /pubmed/35308404 http://dx.doi.org/10.3389/fmicb.2022.837737 Text en Copyright © 2022 Ding, Chen, Chu, Zhong, Huang and Zhang. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Ding, Niannian Chen, Yuanyuan Chu, Yindi Zhong, Cheng Huang, Li Zhang, Zhenfeng Lysine Methylation Modulates the Interaction of Archaeal Chromatin Protein Cren7 With DNA |
title | Lysine Methylation Modulates the Interaction of Archaeal Chromatin Protein Cren7 With DNA |
title_full | Lysine Methylation Modulates the Interaction of Archaeal Chromatin Protein Cren7 With DNA |
title_fullStr | Lysine Methylation Modulates the Interaction of Archaeal Chromatin Protein Cren7 With DNA |
title_full_unstemmed | Lysine Methylation Modulates the Interaction of Archaeal Chromatin Protein Cren7 With DNA |
title_short | Lysine Methylation Modulates the Interaction of Archaeal Chromatin Protein Cren7 With DNA |
title_sort | lysine methylation modulates the interaction of archaeal chromatin protein cren7 with dna |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8927968/ https://www.ncbi.nlm.nih.gov/pubmed/35308404 http://dx.doi.org/10.3389/fmicb.2022.837737 |
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