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Nucleic Acids Research, 1991, Vol. 19, No. 11 3041-3045
© 1991

MOLECULAR BIOLOGY

The chromosomal protein MC1 from the archaebacterium Methanosarcina sp. CHTI 55 induces DNA bending and supercoiling

Bernard Laine*, Françoise Culard1, Jean-Claude Maurizot1 and Pierre Sautiére

Unité de Recherche Associée, 409 au Centre National de la Recherche Scientifique, Institut de Recherches sur le Cancer Place de Verdun, 59045 Lille 1Centre de Biophysique Moleculaire 1A, Avenue de la Recherche Scientifique, 45071 Orleans, France

*To whom correspondence should be addressed

Received January 31, 1991. Revised May 1, 1991. Accepted May 1, 1991.

We have investigated the effect on the DNA structure of protein MC1, a basic and small polypeptide (Mr 10700) representing the major chromosomal protein in Methanosarcinaceae. The ability of protein MC1 to strongly favour cyclization upon polymerization of short DNA fragments by T4 DNA ligase indicates that protein MC1 mediates DNA bending. Several negatively supercoiled topoisomers of minicircles were obtained with DNA fragments of 203 and 146 bp, their distribution depends upon the amount of protein MC1 complexed with DNA. In addition, protein MC1 can induce a compaction of a nicked plasmid.


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F. Toulmé, E. Le Cam, C. Teyssier, E. Delain, P. Sautière, J.-C. Maurizot, and F.ço. Culard
Conformational Changes of DNA Minicircles upon the Binding of the Archaebacterial Histone-like Protein MC1
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