» Articles » PMID: 18515342

DNA Protection by Histone-like Protein HU from the Hyperthermophilic Eubacterium Thermotoga Maritima

Overview
Specialty Biochemistry
Date 2008 Jun 3
PMID 18515342
Citations 18
Authors
Affiliations
Soon will be listed here.
Abstract

In mesophilic prokaryotes, the DNA-binding protein HU participates in nucleoid organization as well as in regulation of DNA-dependent processes. Little is known about nucleoid organization in thermophilic eubacteria. We show here that HU from the hyperthermophilic eubacterium Thermotoga maritima HU bends DNA and constrains negative DNA supercoils in the presence of topoisomerase I. However, while binding to a single site occludes approximately 35 bp, association of T. maritima HU with DNA of sufficient length to accommodate multiple protomers results in an apparent shorter occluded site size. Such complexes consist of ordered arrays of protomers, as revealed by the periodicity of DNase I cleavage. Association of TmHU with plasmid DNA yields a complex that is remarkably resistant to DNase I-mediated degradation. TmHU is the only member of this protein family capable of occluding a 35 bp nonspecific site in duplex DNA; we propose that this property allows TmHU to form exceedingly stable associations in which DNA flanking the kinks is sandwiched between adjacent proteins. We suggest that T. maritima HU serves an architectural function when associating with a single 35 bp site, but generates a very stable and compact aggregate at higher protein concentrations that organizes and protects the genomic DNA.

Citing Articles

G-quadruplex structures in 16S rRNA regions correlate with thermal adaptation in prokaryotes.

Lyu B, Niu K, Anderson D, Feng Q, Song Q Nucleic Acids Res. 2025; 53(3).

PMID: 39883013 PMC: 11780868. DOI: 10.1093/nar/gkaf042.


Molecular and structural basis of an ATPase-nuclease dual-enzyme anti-phage defense complex.

An Q, Wang Y, Tian Z, Han J, Li J, Liao F Cell Res. 2024; 34(8):545-555.

PMID: 38834762 PMC: 11291478. DOI: 10.1038/s41422-024-00981-w.


IHF and Fis as Cell Cycle Regulators: Activation of the Replication Origin and the Regulatory Cycle of the DnaA Initiator.

Kasho K, Ozaki S, Katayama T Int J Mol Sci. 2023; 24(14).

PMID: 37511331 PMC: 10380432. DOI: 10.3390/ijms241411572.


Isolation and Staining Reveal the Presence of Extracellular DNA in Marine Gel Particles.

Al-Wahaibi A, Upstill-Goddard R, Burgess J Gels. 2023; 9(3).

PMID: 36975700 PMC: 10048003. DOI: 10.3390/gels9030251.


Enhanced binding of an HU homologue under increased DNA supercoiling preserves chromosome organisation and sustains Streptomyces hyphal growth.

Strzalka A, Kois-Ostrowska A, Kedra M, Lebkowski T, Bieniarz G, Szafran M Nucleic Acids Res. 2022; 50(21):12202-12216.

PMID: 36420903 PMC: 9756944. DOI: 10.1093/nar/gkac1093.


References
1.
Pavlicek J, Oussatcheva E, Sinden R, Potaman V, Sankey O, Lyubchenko Y . Supercoiling-induced DNA bending. Biochemistry. 2004; 43(33):10664-8. DOI: 10.1021/bi0362572. View

2.
Depew D, Wang J . Conformational fluctuations of DNA helix. Proc Natl Acad Sci U S A. 1975; 72(11):4275-9. PMC: 388703. DOI: 10.1073/pnas.72.11.4275. View

3.
Bocchetta M, Gribaldo S, Sanangelantoni A, CAMMARANO P . Phylogenetic depth of the bacterial genera Aquifex and Thermotoga inferred from analysis of ribosomal protein, elongation factor, and RNA polymerase subunit sequences. J Mol Evol. 2000; 50(4):366-80. DOI: 10.1007/s002399910040. View

4.
Azam T, Ishihama A . Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity. J Biol Chem. 1999; 274(46):33105-13. DOI: 10.1074/jbc.274.46.33105. View

5.
Dame R, Noom M, Wuite G . Bacterial chromatin organization by H-NS protein unravelled using dual DNA manipulation. Nature. 2006; 444(7117):387-90. DOI: 10.1038/nature05283. View