Abstract
In prokaryotic cells, genomic DNA forms an aggregated structure with various nucleoid-associated proteins (NAPs). The functions of genomic DNA are cooperatively modulated by NAPs, of which HU is considered to be one of the most important. HU binds double-stranded DNA (dsDNA) and serves as a structural modulator in the genome architecture. It plays important roles in diverse DNA functions, including replication, segregation, transcription and repair. Interestingly, it has been reported that HU also binds single-stranded DNA (ssDNA) regardless of sequence. However, structural analysis of HU with ssDNA has been lacking, and the functional relevance of this binding remains elusive.In this study, we found that ssDNA induced a significant change in the secondary structure of Thermus thermophilus HU (TtHU), as observed by analysis of circular dichroism spectra. Notably, this change in secondary structure was sequence specific, because the complementary ssDNA or dsDNA did not induce the change. Structural analysis using nuclear magnetic resonance confirmed that TtHU and this ssDNA formed a unique structure, which was different from the previously reported structure of HU in complex with dsDNA. Our data suggest that TtHU undergoes a distinct structural change when it associates with ssDNA of a specific sequence and subsequently exerts a yet-to-be-defined function.
Highlights
In prokaryotic cells, genomic DNA forms an aggregated structure with various nucleoid-associated proteins (NAPs) [1]
We found that single-stranded DNA (ssDNA) induced a significant change in the secondary structure of Thermus thermophilus HU (TtHU), as observed by analysis of circular dichroism spectra
Our data suggest that TtHU undergoes a distinct structural change when it associates with ssDNA of a specific sequence and subsequently exerts a yet-to-be-defined function
Summary
Genomic DNA forms an aggregated structure with various nucleoid-associated proteins (NAPs) [1]. The functions of genomic DNA, such as replication, segregation, translation and repair, are related to its distinct structure, which is cooperatively modulated by NAPs [4,5,6,7]. Mutation in the HU gene and gene disruption of HU affect cell growth or is lethal [11,12]. These results have suggested that HU has a central role among NAPs. HU is a small protein consisting of approximately 90 amino acid residues and mainly exists as a dimer in solution [13]. Some structures of HU alone and in complex with dsDNA have been
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