Stoichiometry of the binding of chromosomal protein MC1 from the archaebacterium, Methanosarcina spp. CHTI55, to DNA.
We have investigated the binding stoichiometry of the chromosomal MC1 protein on DNA using the gel retardation technique. Analysis of the distribution of the complex containing 0, 1, 2, 3 ... bound proteins shows that the protein MC1 interacts with the DNA as a monomer. Binding experiments with short DNA fragments of various lengths shows that the site size is 11 bp in length. These results are compared to those obtained with other chromosomal proteins including HU protein.
Culard
F
F
Centre de biophysique moléculaire, Orléans, France.
Laine
B
B
Sautière
P
P
Maurizot
J C
JC
D019843:Archaeal Proteins; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D004269:DNA, Bacterial / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D017020:Methanosarcina / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000378:metabolism*
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; C051211:HMb protein, Methanosarcina; D012261:Ribonucleoproteins