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...

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Autores principales: Ding, Niannian, Chen, Yuanyuan, Chu, Yindi, Zhong, Cheng, Huang, Li, Zhang, Zhenfeng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
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.
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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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