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• W2046175563 abstract "Architectural DNA proteins play important roles in the chromosomal DNA organization and global gene regulation in living cells. However, physiological functions of some DNA-binding proteins from archaea remain unclear. Recently, several abundant DNA-architectural proteins including histones, Alba, and TrmBL2 have been identified in model euryarchaeon Thermococcus kodakarensis. Although histones and Alba proteins have been previously characterized, the DNA binding properties of TrmBL2 and its interplay with the other major architectural proteins in the chromosomal DNA organization and gene transcription regulation remain largely unexplored. Here, we report single-DNA studies showing that at low ionic strength (<300 mm KCl), TrmBL2 binds to DNA largely in non-sequence-specific manner with positive cooperativity, resulting in formation of stiff nucleoprotein filamentous patches, whereas at high ionic strength (>300 mm KCl) TrmBL2 switches to more sequence-specific interaction, suggesting the presence of high affinity TrmBL2-filament nucleation sites. Furthermore, in vitro assays indicate the existence of DNA binding competition between TrmBL2 and archaeal histones B from T. kodakarensis, which can be strongly modulated by DNA supercoiling and ionic strength of surrounding solution. Overall, these results advance our understanding of TrmBL2 DNA binding properties and provide important insights into potential functions of architectural proteins in nucleoid organization and gene regulation in T. kodakarensis.Background:TrmBL2 and histones maintain the genome functioning in hyperthermophilic euryarchaeal cells.Results:TrmBL2 forms filaments on DNA through cooperative binding and competes with histones in a salt- and DNA supercoiling-dependent manner.Conclusion:TrmBL2-histone collective behavior dynamically controls DNA organization.Significance:The discovered mechanisms provide insights into the regulation of the genome structure and global transcription profile by TrmBL2 and histones. Architectural DNA proteins play important roles in the chromosomal DNA organization and global gene regulation in living cells. However, physiological functions of some DNA-binding proteins from archaea remain unclear. Recently, several abundant DNA-architectural proteins including histones, Alba, and TrmBL2 have been identified in model euryarchaeon Thermococcus kodakarensis. Although histones and Alba proteins have been previously characterized, the DNA binding properties of TrmBL2 and its interplay with the other major architectural proteins in the chromosomal DNA organization and gene transcription regulation remain largely unexplored. Here, we report single-DNA studies showing that at low ionic strength (<300 mm KCl), TrmBL2 binds to DNA largely in non-sequence-specific manner with positive cooperativity, resulting in formation of stiff nucleoprotein filamentous patches, whereas at high ionic strength (>300 mm KCl) TrmBL2 switches to more sequence-specific interaction, suggesting the presence of high affinity TrmBL2-filament nucleation sites. Furthermore, in vitro assays indicate the existence of DNA binding competition between TrmBL2 and archaeal histones B from T. kodakarensis, which can be strongly modulated by DNA supercoiling and ionic strength of surrounding solution. Overall, these results advance our understanding of TrmBL2 DNA binding properties and provide important insights into potential functions of architectural proteins in nucleoid organization and gene regulation in T. kodakarensis. TrmBL2 and histones maintain the genome functioning in hyperthermophilic euryarchaeal cells. TrmBL2 forms filaments on DNA through cooperative binding and competes with histones in a salt- and DNA supercoiling-dependent manner. TrmBL2-histone collective behavior dynamically controls DNA organization." @default.
• W2046175563 created "2016-06-24" @default.
• W2046175563 creator A5029928652 @default.
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• W2046175563 date "2015-06-01" @default.
• W2046175563 modified "2023-09-30" @default.
• W2046175563 title "Transcriptional Repressor TrmBL2 from Thermococcus kodakarensis Forms Filamentous Nucleoprotein Structures and Competes with Histones for DNA Binding in a Salt- and DNA Supercoiling-dependent Manner" @default.
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• W2046175563 doi "https://doi.org/10.1074/jbc.m114.626705" @default.
• W2046175563 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4505486" @default.
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