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Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein
DNA mimic proteins are unique factors that control the DNA-binding activity of target proteins by directly occupying their DNA-binding sites. To date, only a few DNA mimic proteins have been reported and their functions analyzed. Here, we present evidence that the Neisseria conserved hypothetical pr...
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/PMC3643605/ https://www.ncbi.nlm.nih.gov/pubmed/23531546 http://dx.doi.org/10.1093/nar/gkt201 |
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author | Wang, Hao-Ching Wu, Mao-Lun Ko, Tzu-Ping Wang, Andrew H.-J. |
author_facet | Wang, Hao-Ching Wu, Mao-Lun Ko, Tzu-Ping Wang, Andrew H.-J. |
author_sort | Wang, Hao-Ching |
collection | PubMed |
description | DNA mimic proteins are unique factors that control the DNA-binding activity of target proteins by directly occupying their DNA-binding sites. To date, only a few DNA mimic proteins have been reported and their functions analyzed. Here, we present evidence that the Neisseria conserved hypothetical protein DMP12 should be added to this list. Our gel filtration and analytical ultracentrifugation results showed that the DMP12 monomer interacts with the dimeric form of the bacterial histone-like protein HU. Subsequent structural analysis of DMP12 showed that the shape and electrostatic surface of the DMP12 monomer are similar to those of the straight portion of the bent HU-bound DNA and complementary to those of HU protein dimer. DMP12 also protects HU protein from limited digestion by trypsin and enhances the growth rate Escherichia coli. Functionally, HU proteins participate in bacterial nucleoid formation, as well as recombination, gene regulation and DNA replication. The interaction between DMP12 and HU protein might, therefore, play important roles in these DNA-related mechanisms. |
format | Online Article Text |
id | pubmed-3643605 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-36436052013-05-03 Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein Wang, Hao-Ching Wu, Mao-Lun Ko, Tzu-Ping Wang, Andrew H.-J. Nucleic Acids Res Structural Biology DNA mimic proteins are unique factors that control the DNA-binding activity of target proteins by directly occupying their DNA-binding sites. To date, only a few DNA mimic proteins have been reported and their functions analyzed. Here, we present evidence that the Neisseria conserved hypothetical protein DMP12 should be added to this list. Our gel filtration and analytical ultracentrifugation results showed that the DMP12 monomer interacts with the dimeric form of the bacterial histone-like protein HU. Subsequent structural analysis of DMP12 showed that the shape and electrostatic surface of the DMP12 monomer are similar to those of the straight portion of the bent HU-bound DNA and complementary to those of HU protein dimer. DMP12 also protects HU protein from limited digestion by trypsin and enhances the growth rate Escherichia coli. Functionally, HU proteins participate in bacterial nucleoid formation, as well as recombination, gene regulation and DNA replication. The interaction between DMP12 and HU protein might, therefore, play important roles in these DNA-related mechanisms. Oxford University Press 2013-05 2013-03-26 /pmc/articles/PMC3643605/ /pubmed/23531546 http://dx.doi.org/10.1093/nar/gkt201 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 | Structural Biology Wang, Hao-Ching Wu, Mao-Lun Ko, Tzu-Ping Wang, Andrew H.-J. Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein |
title | Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein |
title_full | Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein |
title_fullStr | Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein |
title_full_unstemmed | Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein |
title_short | Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein |
title_sort | neisseria conserved hypothetical protein dmp12 is a dna mimic that binds to histone-like hu protein |
topic | Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3643605/ https://www.ncbi.nlm.nih.gov/pubmed/23531546 http://dx.doi.org/10.1093/nar/gkt201 |
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