The monomeric form of Neisseria DNA mimic protein DMP19 prevents DNA from binding to the histone-like HU protein

Ming Fen Huang, Shin Jen Lin, Tzu Ping Ko, Yi Ting Liao, Kai Cheng Hsu, Hao Ching Wang

研究成果: 雜誌貢獻文章

4 引文 (Scopus)

摘要

DNA mimicry is a direct and effective strategy by which the mimic competes with DNA for the DNA binding sites on other proteins. Until now, only about a dozen proteins have been shown to function via this strategy, including the DNA mimic protein DMP19 from Neisseria meningitides. We have shown previously that DMP19 dimer prevents the operator DNA from binding to the transcription factor NHTF. Here, we provide new evidence that DMP19 monomer can also interact with the Neisseria nucleoid-associated protein HU. Using BS3 crosslinking, gel filtration and isothermal titration calorimetry assays, we found that DMP19 uses its monomeric form to interact with the Neisseria HU dimer. Crosslinking conjugated mass spectrometry was used to investigate the binding mode of DMP19 monomer and HU dimer. Finally, an electrophoretic mobility shift assay (EMSA) confirmed that the DNA binding affinity of HU is affected by DMP19. These results showed that DMP19 is bifunctional in the gene regulation of Neisseria through its variable oligomeric forms.
原文英語
文章編號e0189461
期刊PLoS One
12
發行號12
DOIs
出版狀態已發佈 - 十二月 1 2017

指紋

Neisseria
histones
Histones
DNA
Dimers
Proteins
proteins
crosslinking
Crosslinking
Assays
Molecular Mimicry
Monomers
Calorimetry
Electrophoretic Mobility Shift Assay
Electrophoretic mobility
Meningitis
operator regions
meningitis
calorimetry
Gel Chromatography

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

引用此文

The monomeric form of Neisseria DNA mimic protein DMP19 prevents DNA from binding to the histone-like HU protein. / Huang, Ming Fen; Lin, Shin Jen; Ko, Tzu Ping; Liao, Yi Ting; Hsu, Kai Cheng; Wang, Hao Ching.

於: PLoS One, 卷 12, 編號 12, e0189461, 01.12.2017.

研究成果: 雜誌貢獻文章

@article{27ab413ec28e4a109923cc5211905bc5,
title = "The monomeric form of Neisseria DNA mimic protein DMP19 prevents DNA from binding to the histone-like HU protein",
abstract = "DNA mimicry is a direct and effective strategy by which the mimic competes with DNA for the DNA binding sites on other proteins. Until now, only about a dozen proteins have been shown to function via this strategy, including the DNA mimic protein DMP19 from Neisseria meningitides. We have shown previously that DMP19 dimer prevents the operator DNA from binding to the transcription factor NHTF. Here, we provide new evidence that DMP19 monomer can also interact with the Neisseria nucleoid-associated protein HU. Using BS3 crosslinking, gel filtration and isothermal titration calorimetry assays, we found that DMP19 uses its monomeric form to interact with the Neisseria HU dimer. Crosslinking conjugated mass spectrometry was used to investigate the binding mode of DMP19 monomer and HU dimer. Finally, an electrophoretic mobility shift assay (EMSA) confirmed that the DNA binding affinity of HU is affected by DMP19. These results showed that DMP19 is bifunctional in the gene regulation of Neisseria through its variable oligomeric forms.",
author = "Huang, {Ming Fen} and Lin, {Shin Jen} and Ko, {Tzu Ping} and Liao, {Yi Ting} and Hsu, {Kai Cheng} and Wang, {Hao Ching}",
year = "2017",
month = "12",
day = "1",
doi = "10.1371/journal.pone.0189461",
language = "English",
volume = "12",
journal = "PLoS One",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "12",

}

TY - JOUR

T1 - The monomeric form of Neisseria DNA mimic protein DMP19 prevents DNA from binding to the histone-like HU protein

AU - Huang, Ming Fen

AU - Lin, Shin Jen

AU - Ko, Tzu Ping

AU - Liao, Yi Ting

AU - Hsu, Kai Cheng

AU - Wang, Hao Ching

PY - 2017/12/1

Y1 - 2017/12/1

N2 - DNA mimicry is a direct and effective strategy by which the mimic competes with DNA for the DNA binding sites on other proteins. Until now, only about a dozen proteins have been shown to function via this strategy, including the DNA mimic protein DMP19 from Neisseria meningitides. We have shown previously that DMP19 dimer prevents the operator DNA from binding to the transcription factor NHTF. Here, we provide new evidence that DMP19 monomer can also interact with the Neisseria nucleoid-associated protein HU. Using BS3 crosslinking, gel filtration and isothermal titration calorimetry assays, we found that DMP19 uses its monomeric form to interact with the Neisseria HU dimer. Crosslinking conjugated mass spectrometry was used to investigate the binding mode of DMP19 monomer and HU dimer. Finally, an electrophoretic mobility shift assay (EMSA) confirmed that the DNA binding affinity of HU is affected by DMP19. These results showed that DMP19 is bifunctional in the gene regulation of Neisseria through its variable oligomeric forms.

AB - DNA mimicry is a direct and effective strategy by which the mimic competes with DNA for the DNA binding sites on other proteins. Until now, only about a dozen proteins have been shown to function via this strategy, including the DNA mimic protein DMP19 from Neisseria meningitides. We have shown previously that DMP19 dimer prevents the operator DNA from binding to the transcription factor NHTF. Here, we provide new evidence that DMP19 monomer can also interact with the Neisseria nucleoid-associated protein HU. Using BS3 crosslinking, gel filtration and isothermal titration calorimetry assays, we found that DMP19 uses its monomeric form to interact with the Neisseria HU dimer. Crosslinking conjugated mass spectrometry was used to investigate the binding mode of DMP19 monomer and HU dimer. Finally, an electrophoretic mobility shift assay (EMSA) confirmed that the DNA binding affinity of HU is affected by DMP19. These results showed that DMP19 is bifunctional in the gene regulation of Neisseria through its variable oligomeric forms.

UR - http://www.scopus.com/inward/record.url?scp=85037652565&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85037652565&partnerID=8YFLogxK

U2 - 10.1371/journal.pone.0189461

DO - 10.1371/journal.pone.0189461

M3 - Article

C2 - 29220372

AN - SCOPUS:85037652565

VL - 12

JO - PLoS One

JF - PLoS One

SN - 1932-6203

IS - 12

M1 - e0189461

ER -