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Journal of Bacteriology, July 2000, p. 3929-3933, Vol. 182, No. 14
State Key Laboratory of Microbial Resources,
Institute of Microbiology, Chinese Academy of Sciences, Beijing
100080, People's Republic of China
Received 20 December 1999/Accepted 4 May 2000
The DNA binding protein Ssh10b, a member of the Sac10b family, has
been purified from the hyperthermophilic archaeon Sulfolobus shibatae. Ssh10b constitutes about 4% of the cellular protein. Electrophoretic mobility shift assays showed that Ssh10b first bound a
double-stranded DNA fragment with an estimated binding size of
~~12 bp, forming distinct shifts, until the DNA was
coated with the protein. Binding of more Ssh10b resulted in the
formation of smears of lower mobilities. The migration pattern of the
smearing Ssh10b-DNA complexes was affected by temperature, whereas that of complexes associated with the distinct shifts was not.
Interestingly, Ssh10b was capable of constraining negative DNA
supercoils in a temperature-dependent fashion. While the ability of the
protein to constrain supercoils was weak at 25°C, it was enhanced
substantially at 45°C or higher temperatures (up to 80°C). Taken
together, our data suggest that archaeal proteins of the Sac10b family
may affect the topology of chromosomal DNA in thermophilic archaea at
their growth temperatures.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
An Abundant DNA Binding Protein from the
Hyperthermophilic Archaeon Sulfolobus shibatae Affects DNA
Supercoiling in a Temperature-Dependent Fashion
*
Corresponding author. Mailing address: State Key
Laboratory of Microbial Resources, Institute of Microbiology, Chinese
Academy of Sciences, Beijing 100080, People's Republic of China.
Phone: 86-10-62624971. Fax: 86-10-62560912. E-mail:
huangl{at}sun.im.ac.cn.
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