Atypical Recognition of Particular DNA Sequences by the Archaeal Chromosomal MC1 Protein

• Published in: Biochemistry (Easton) Vol. 44; no. 30; pp. 10369 - 10377
• Main Authors: De Vuyst, Guillaume, Aci, Samia, Genest, Daniel, Culard, Françoise
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 02-08-2005
• Subjects: Archaea; Archaeal Proteins - chemistry; Archaeal Proteins - metabolism; Binding Sites; Chromosomal Proteins, Non-Histone - chemistry; Chromosomal Proteins, Non-Histone - metabolism; Consensus Sequence; DNA, Archaeal - chemistry; DNA, Archaeal - metabolism; Gene Library; Methanosarcina; Nucleic Acid Heteroduplexes - chemistry; Nucleic Acid Heteroduplexes - metabolism; Protein Conformation; Ribonucleoproteins - chemistry; Ribonucleoproteins - metabolism; Sequence Alignment; Thermodynamics
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi0474416

The MC1 protein is a chromosomal protein likely involved in the DNA compaction of some methanogenic archaea. This small and monomeric protein, structurally unrelated to other DNA binding proteins, bends DNA sharply. By studying the protein binding to various kinds of kinked DNA, we have previously shown that MC1 is able to discriminate between different deformations of the DNA helix. Here we investigate its capacity to recognize particular DNA sequences by using a SELEX procedure. We find that MC1 is able to preferentially bind to a 15 base pair motif [AAAAACACAC(A/C)CCCC]. The structural parameters of this sequence are characterized by molecular dynamics simulation experiments, and the binding mode of the protein to the DNA is studied by footprinting experiments. Our results strongly suggest that the protein realizes an indirect readout of the DNA sequence by binding to the DNA minor groove.