Structure-specific binding recognition of a methanogen chromosomal protein.
The archaeon Methanosarcina thermophila expresses large amounts of a small basic protein, called MC1 (methanogen chromosomal protein), which was previously identified as a DNA-binding protein possibly involved in DNA compaction in some methanogenic species. We have investigated the binding of MC1 to various kinds of branched DNA molecules whose double helix axis is severely kinked. We show that MC1 is able to distinguish and to bind preferentially to four-way junctions. This preferential binding is observed in the absence and presence of divalent cations. However, we find that MC1 has a low affinity for bulged DNA structures. These results show how MC1 is able to discriminate between different deformations of the DNA double helix.
Paradinas
C
C
Centre de Biophysique Moléculaire conventionné par l'université d'Orléans, France.
Gervais
A
A
Maurizot
J C
JC
Culard
F
F
D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism*; D001483:Base Sequence; D001665:Binding Sites; D004269:DNA, Bacterial / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D015636:Magnesium Chloride / Q000737:chemistry; D017020:Methanosarcina / Q000378:metabolism*; D015335:Molecular Probes; D011487:Protein Conformation; D012261:Ribonucleoproteins / Q000737:chemistry / Q000378:metabolism*
D019843:Archaeal Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; C051211:HMb protein, Methanosarcina; D015335:Molecular Probes; D012261:Ribonucleoproteins; D015636:Magnesium Chloride