A specific single-stranded DNA induces a distinct conformational change in the nucleoid-associated protein HU

Yuya Nishida, Teppei Ikeya, Tsutomu Mikawa, Jin Inoue, Yutaka Ito, Yasunori Shintani, Ryoji Masui, Seiki Kuramitsu, Seiji Takashima

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)318-324
Number of pages7
JournalBiochemistry and Biophysics Reports
Publication statusPublished - 2016 Dec 1
Externally publishedYes


  • Circular dichroism
  • HU
  • NMR
  • Nucleoid-associated protein
  • Single-stranded DNA
  • Thermus

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry


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