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J. Biol. Chem., Vol. 276, Issue 14, 10745-10752, April 6, 2001
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From the In hyperthermophilic Archaea genomic DNA
is from relaxed to positively supercoiled in vivo because
of the action of the enzyme reverse gyrase, and this peculiarity is
believed to be related to stabilization of DNA against denaturation. We
report the identification and characterization of Smj12, a novel
protein of Sulfolobus solfataricus, which is homologous to
members of the so-called Bacterial-Archaeal family of regulators, found
in multiple copies in Eubacteria and Archaea. Whereas other members of
the family are sequence-specific DNA- binding proteins and have been
implicated in transcriptional regulation, Smj12 is a nonspecific
DNA-binding protein that stabilizes the double helix and induces
positive supercoiling. Smj12 is not abundant, suggesting that it is not
a general architectural protein, but rather has a specialized function
and/or localization. Smj12 is the first protein with the described
features identified in Archaea and might participate in control of
superhelicity during DNA transactions.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ133494.
A Novel Member of the Bacterial-Archaeal Regulator Family Is
a Nonspecific DNA-binding Protein and Induces Positive
Supercoiling*
,, and¶
Institute of Protein Biochemistry and
Enzymology, Consiglio Nazionale delle Ricerche, Via Marconi 10, 80125 Naples, Italy and the § Centre for Biomolecular Science, St.
Andrews University, KY16 9ST, St. Andrews, United
Kingdom
*
This work was partially supported by the European Union
project "Extremophiles as cell factories" and by the CNR Special
Program "Biomolecole per la salute umana."The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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