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Stoichiometry of the binding of chromosomal protein MCl from the archaebacterium, Methanosarcina spp. CHTI55, to DNA
Author(s) -
Culard Françoise,
Laine Bernard,
Sautiére Pierre,
Maurizot JeanClaude
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81189-7
Subject(s) - dna , monomer , stoichiometry , dna binding protein , biology , microbiology and biotechnology , plasma protein binding , chemistry , biochemistry , biophysics , gene , transcription factor , organic chemistry , polymer
We have investigated the binding Stoichiometry of the chromosomal MCl 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 MCl 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.