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Nucleoid-associated proteins (NAPs) or histone-like proteins (HLPs) are DNA-binding proteins present in bacteria that play an important role in nucleoid architecture and gene regulation. NAPs affect bacterial nucleoid organization via DNA bending, bridging, or forming aggregates. EbfC is a nucleoid-associated protein identified first in  Borrelia burgdorferi , belonging to YbaB/EbfC family of NAPs capable of binding and altering DNA conformation. YbaB, an ortholog of EbfC found in  Escherichia coli  and  Haemophilus influenzae , also acts as a transcriptional regulator. YbaB has a novel tweezer-like structure and binds DNA as homodimers. The homologs of YbaB are found in almost all bacterial species, suggesting a conserved function, yet the physiological role of YbaB protein in many bacteria is not well understood. In this study, we characterized the YbaB/EbfC family DNA-binding protein in  Caulobacter crescentus. C. crescentus  has one YbaB/EbfC family gene annotated in the genome (YbaB  C    c  ) and it shares 41% sequence identity with YbaB/EbfC family NAPs. Computational modeling revealed tweezer-like structure of YbaB  C    c  , a characteristic of YbaB/EbfC family of NAPs. N-terminal–CFP tagged YbaB  C    c   localized with the nucleoid and is able to compact DNA. Unlike  B. burgdorferi  EbfC protein, YbaB  C    c   protein is a non-specific DNA-binding protein in  C. crescentus . Moreover, YbaB  C    c   shields DNA against enzymatic degradation. Collectively, our findings reveal that YbaB  C    c   is a small histone-like protein and may play a role in bacterial chromosome structuring and gene regulation in  C. crescentus.

DNA-Binding Properties of YbaB, a Putative Nucleoid-Associated Protein From Caulobacter crescentus