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J. Biol. Chem., Vol. 276, Issue 14, 10745-10752, April 6, 2001
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,
, and
¶
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.
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
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ133494.
¶ To whom correspondence should be addressed. Tel.: 390817257246; Fax: 390812396525; E-mail: ciaramel@dafne.ibpe.na.cnr.it.This article has been cited by other articles:
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