Proteins from the Prokaryotic Nucleoid: Biochemical and 1H NMR Studies on Three Bacterial Histone-Like Proteins

• DOI: 10.1007/978-1-4684-8730-5_48
• Publication Date: 2013-06-01T06:48:24Z
• Authors: M. Lammi; M. Paci; C. L. Pon; M. A. Losso; A. Miano; R. T. Pawlik; G. L. Gianfranceschi; C. O. Gualerzi
• Keywords: DNA-Binding Proteins; Hot Temperature; Magnetic Resonance Spectroscopy; Bacterial Proteins; Transcription, Genetic; Protein Conformation; Escherichia coli; Animals; Cattle; DNA; In Vitro Techniques; Nucleic Acid Denaturation; Protein Binding

In the past, the absence of histones and organized chromatin were regarded as characteristics of the prokaryotic cell. In reality, the approximately 4000 kb circular chromosome of bacteria is condensed in a region called the nucleoid and gentle lysis methods allowed the obtainment of chromatin-like fibers with repetitive granular structure. The granules have a diameter ≃ 130 A and are reminiscent of the eukaryotic nucleosome (1). In the structural organization of “bacterial chromatin”, a role is probably played by specific DNA-binding proteins (2–5). Only recently, the characterization of the structural and functional properties of these proteins has been undertaken in various laboratories.