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Mechanism of DNA organization by Mycobacterium tuberculosis protein Lsr2
Bacterial nucleoid-associated proteins, such as H-NS-like proteins in Enterobacteriaceae, are abundant DNA-binding proteins that function in chromosomal DNA organization and gene transcription regulation. The Mycobacterium tuberculosis Lsr2 protein has been proposed to be the first identified H-NS a...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3664827/ https://www.ncbi.nlm.nih.gov/pubmed/23580555 http://dx.doi.org/10.1093/nar/gkt249 |
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author | Qu, Yuanyuan Lim, Ci Ji Whang, Yixun R. Liu, Jun Yan, Jie |
author_facet | Qu, Yuanyuan Lim, Ci Ji Whang, Yixun R. Liu, Jun Yan, Jie |
author_sort | Qu, Yuanyuan |
collection | PubMed |
description | Bacterial nucleoid-associated proteins, such as H-NS-like proteins in Enterobacteriaceae, are abundant DNA-binding proteins that function in chromosomal DNA organization and gene transcription regulation. The Mycobacterium tuberculosis Lsr2 protein has been proposed to be the first identified H-NS analogue in Gram-positive bacteria based on its capability to complement numerous in vivo functions of H-NS. Here, we report that Lsr2 cooperatively binds to DNA forming a rigid Lsr2 nucleoprotein complex that restricts DNA accessibility, similar to H-NS. On large DNA, the rigid Lsr2 nucleoprotein complexes can mediate DNA condensation into highly compact DNA conformations. In addition, the responses of Lsr2 nucleoprotein complex to environmental factors (salt concentration, temperature and pH) were studied over physiological ranges. These results provide mechanistic insights into how Lsr2 may mediate its gene silencing, genomic DNA protection and organization functions in vivo. Finally, our results strongly support that Lsr2 is an H-NS-like protein in Gram-positive bacteria from a structural perspective. |
format | Online Article Text |
id | pubmed-3664827 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-36648272013-05-28 Mechanism of DNA organization by Mycobacterium tuberculosis protein Lsr2 Qu, Yuanyuan Lim, Ci Ji Whang, Yixun R. Liu, Jun Yan, Jie Nucleic Acids Res Gene Regulation, Chromatin and Epigenetics Bacterial nucleoid-associated proteins, such as H-NS-like proteins in Enterobacteriaceae, are abundant DNA-binding proteins that function in chromosomal DNA organization and gene transcription regulation. The Mycobacterium tuberculosis Lsr2 protein has been proposed to be the first identified H-NS analogue in Gram-positive bacteria based on its capability to complement numerous in vivo functions of H-NS. Here, we report that Lsr2 cooperatively binds to DNA forming a rigid Lsr2 nucleoprotein complex that restricts DNA accessibility, similar to H-NS. On large DNA, the rigid Lsr2 nucleoprotein complexes can mediate DNA condensation into highly compact DNA conformations. In addition, the responses of Lsr2 nucleoprotein complex to environmental factors (salt concentration, temperature and pH) were studied over physiological ranges. These results provide mechanistic insights into how Lsr2 may mediate its gene silencing, genomic DNA protection and organization functions in vivo. Finally, our results strongly support that Lsr2 is an H-NS-like protein in Gram-positive bacteria from a structural perspective. Oxford University Press 2013-05 2013-04-10 /pmc/articles/PMC3664827/ /pubmed/23580555 http://dx.doi.org/10.1093/nar/gkt249 Text en © The Author(s) 2013. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Gene Regulation, Chromatin and Epigenetics Qu, Yuanyuan Lim, Ci Ji Whang, Yixun R. Liu, Jun Yan, Jie Mechanism of DNA organization by Mycobacterium tuberculosis protein Lsr2 |
title | Mechanism of DNA organization by Mycobacterium tuberculosis protein Lsr2 |
title_full | Mechanism of DNA organization by Mycobacterium tuberculosis protein Lsr2 |
title_fullStr | Mechanism of DNA organization by Mycobacterium tuberculosis protein Lsr2 |
title_full_unstemmed | Mechanism of DNA organization by Mycobacterium tuberculosis protein Lsr2 |
title_short | Mechanism of DNA organization by Mycobacterium tuberculosis protein Lsr2 |
title_sort | mechanism of dna organization by mycobacterium tuberculosis protein lsr2 |
topic | Gene Regulation, Chromatin and Epigenetics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3664827/ https://www.ncbi.nlm.nih.gov/pubmed/23580555 http://dx.doi.org/10.1093/nar/gkt249 |
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