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Papers In Press, published online ahead of print January 8, 2001
Intitute of Protein Biochemistry and Enzymology, National Research Council, I-80125, Naples
Corresponding Author: ciaramel{at}dafne.ibpe.na.cnr.it
In hyperthermophilic Archaea genomic DNA is from relaxed to positively supercoiled in vivo, due to the action of the enzyme reverse gyrase, and this peculiarity is believed to be related to stabilisation of DNA against denaturation. We report the identification and characterisation 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 non-specific DNA binding protein which stabilises the double helix and induces positive supercoiling. Smj12 is not abundant, suggesting that it is not a general architectural protein, but rather has a specialised function and/or localisation. Smj12 is the first protein with the described features identified in Archaea and might participate in control of superhelicity during DNA transactions.
J. Biol. Chem, 10.1074/jbc.M010611200
Submitted on November 26, 2000
Revised on January 4, 2001
Accepted on January 8, 2001
A novel member of the Bacterial-Archaeal regulator family is a non-specific DNA binding protein and induces positive supercoiling
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