Conformation of DNA in chromatin protein-DNA complexes studied by infrared spectroscopy. 1979

J Liquier, and M C Gadenne, and E Taillandier, and N Defer, and F Favatier, and J Kruh

The following observations concerning the DNA secondary structures in various nucleohistone complexes were made by infrared spectroscopy: 1/ in chromatin, chromatin extracted by 0.6 M NaCl, nucleosomes, and histone-DNA reconstituted complexes, the DNA remains in a B type conformation at low relative hygrometry; 2/ in chromatin extracted by tRNA and in non histone protein-DNA reconstituted complexes, the DNA can adopt an A type conformation. Infrared linear dichroism data show that in NHP-DNA complexes the low relative hygrometry conformation of DNA may be modified and that the infrared parameter -1090 is close to that measured for RNA's or DNA-RNA hybrids. It is concluded that the histones block the DNA in a B form and that some of the NHP could be involved in the control of the secondary structure of DNA in chromatin.

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D009690 Nucleic Acid Conformation The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape. DNA Conformation,RNA Conformation,Conformation, DNA,Conformation, Nucleic Acid,Conformation, RNA,Conformations, DNA,Conformations, Nucleic Acid,Conformations, RNA,DNA Conformations,Nucleic Acid Conformations,RNA Conformations
D009698 Nucleoproteins Proteins conjugated with nucleic acids. Nucleoprotein
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D002467 Cell Nucleus Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed) Cell Nuclei,Nuclei, Cell,Nucleus, Cell
D002843 Chromatin The material of CHROMOSOMES. It is a complex of DNA; HISTONES; and nonhistone proteins (CHROMOSOMAL PROTEINS, NON-HISTONE) found within the nucleus of a cell. Chromatins
D002868 Chromosomal Proteins, Non-Histone Nucleoproteins, which in contrast to HISTONES, are acid insoluble. They are involved in chromosomal functions; e.g. they bind selectively to DNA, stimulate transcription resulting in tissue-specific RNA synthesis and undergo specific changes in response to various hormones or phytomitogens. Non-Histone Chromosomal Proteins,Chromosomal Proteins, Non Histone,Chromosomal Proteins, Nonhistone,Non-Histone Chromosomal Phosphoproteins,Chromosomal Phosphoproteins, Non-Histone,Non Histone Chromosomal Phosphoproteins,Non Histone Chromosomal Proteins,Nonhistone Chromosomal Proteins,Proteins, Non-Histone Chromosomal
D003852 Deoxyribonucleoproteins Proteins conjugated with deoxyribonucleic acids (DNA) or specific DNA.
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D006657 Histones Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each. Histone,Histone H1,Histone H1(s),Histone H2a,Histone H2b,Histone H3,Histone H3.3,Histone H4,Histone H5,Histone H7

Related Publications

J Liquier, and M C Gadenne, and E Taillandier, and N Defer, and F Favatier, and J Kruh
August 1994, Biochemical Society transactions,
J Liquier, and M C Gadenne, and E Taillandier, and N Defer, and F Favatier, and J Kruh
August 1996, Current opinion in biotechnology,
J Liquier, and M C Gadenne, and E Taillandier, and N Defer, and F Favatier, and J Kruh
November 2020, Analytical chemistry,
J Liquier, and M C Gadenne, and E Taillandier, and N Defer, and F Favatier, and J Kruh
March 2009, Langmuir : the ACS journal of surfaces and colloids,
J Liquier, and M C Gadenne, and E Taillandier, and N Defer, and F Favatier, and J Kruh
January 1994, Biochemistry,
J Liquier, and M C Gadenne, and E Taillandier, and N Defer, and F Favatier, and J Kruh
September 1979, Nucleic acids research,
J Liquier, and M C Gadenne, and E Taillandier, and N Defer, and F Favatier, and J Kruh
September 2013, Colloids and surfaces. B, Biointerfaces,
J Liquier, and M C Gadenne, and E Taillandier, and N Defer, and F Favatier, and J Kruh
January 2014, Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy,
J Liquier, and M C Gadenne, and E Taillandier, and N Defer, and F Favatier, and J Kruh
January 1973, International journal of peptide and protein research,
J Liquier, and M C Gadenne, and E Taillandier, and N Defer, and F Favatier, and J Kruh
September 2001, Biophysical journal,
Copied contents to your clipboard!