The chromosomal protein MC1 from the archaebacterium Methanosarcina sp. CHTI 55 induces DNA bending and supercoiling.
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.
Laine
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B
Unité de Recherche Associée, 409 au Centre National de la Recherche Scientifique, Institut de Recherches sur le Cancer, Lille, France.
Culard
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F
Maurizot
J C
JC
Sautière
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P
D019843:Archaeal Proteins; D001426:Bacterial Proteins / Q000378:metabolism*; D002876:Chromosomes, Bacterial; D011088:DNA Ligases / Q000737:chemistry; D004269:DNA, Bacterial / Q000737:chemistry*; D004278:DNA, Superhelical / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D019605:Euryarchaeota / Q000235:genetics*; D009690:Nucleic Acid Conformation; D012261:Ribonucleoproteins / Q000378:metabolism*
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004278:DNA, Superhelical; C051211:HMb protein, Methanosarcina; D012261:Ribonucleoproteins; D011088:DNA Ligases