Nucleic Acids Research, Vol 26, Issue 10 2322-2328, Copyright © 1998 by Oxford University Press
P Lopez-Garcia, S Knapp, R Ladenstein and P Forterre
The topological state of DNA in hyperthermophilic archaea appears to
correspond to a linking excess in comparison with DNA in mesophilic
organisms. Since DNA binding proteins often contribute to the control of
DNA topology by affecting DNA geometry in the presence of DNA
topoisomerases, we tested whether the histone-like protein Sso7d from the
hyperthermophilic archaeon Sulfolobus solfataricus alters DNA conformation.
In ligase-mediated supercoiling assays carried out at 37, 60, 70, 80 and 90
degrees C we found that DNA binding of increasing amounts of Sso7d led to a
progressive decrease in plasmid linking number (Lk), producing negative
supercoiling. Identical unwinding effects were observed when recombinant
non-methylated Sso7d was used. For a given Sso7d concentration the DNA
unwinding induced was augmented with increasing temperature. However, after
correction for the overwinding effect of high temperature on DNA, plasmids
ligated at 60- 90 degrees C exhibited similar sigma values at the highest
Sso7d concentrations assayed. These results suggest that Sso7d may play a
compensatory role in vivo by counteracting the overwinding effect of high
temperature on DNA. Additionally, Sso7d unwinding could be involved in the
topological changes observed during thermal stress (heat and cold shock),
playing an analogous role in crenarchaeal cells to that proposed for HU in
bacteria.
ARTICLES
In vitro DNA binding of the archaeal protein Sso7d induces negative supercoiling at temperatures typical for thermophilic growth
Institut de Genetique et Microbiologie, Universite Paris-Sud, CNRS URA 1354, GDR 1006, Batiment 409, 91405 Orsay Cedex, France.
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