Single Molecule Studies of DNA-Protamine Interactions
Abstract:Single molecule studies of protamine-DNA interactions have characterized the kinetics of protamine binding to DNA and the morphology of the toroidal subunits that comprise sperm chromatin. The results provided by these studies are reviewed, the advantage of using single molecule techniques is discussed, and the implications of the results to the structure, kinetics of toroid formation, and stability of the DNA-protamine complex are described. New measurements of DNA condensation forces induced by the binding of protamine to DNA are also presented. These forces induce a significant tension in constrained segments of DNA and may contribute to the reduction in volume and shaping of the maturing spermatid cell nucleus.
Keywords: Atomic force microscopy; DNA Condensation Forces; DNA Tension; DNA-protamine complexes; DNA-protamine interactions; DNA-protamine toroids; PROTAMINE BINDING KINETICS; Sigma-Aldrich; Sperm genomic DNA; anchoring domains; chromatin nodules; fertilization; nucleosomes; optical trap; salmon protamine; single molecule; sperm chromatin; spermatid; spermiogenesis; transition protein 1; transmission electron microscopy
Document Type: Research Article
Publication date: August 1, 2011
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.