Neutron scatter studies of chromatin structures related to functions

Technical Report · Tue Jan 01 04:00:00 EST 1991

DOI:https://doi.org/10.2172/6000035· OSTI ID:6000035

Bradbury, E M

We have completed a study on the structure of trypsin trimmed histone octamers using small angle neutron and X-ray scattering studies and nuclear magnetic resonance. We have also completed studies on the structure of TFIIIA induced DNA bending by a circular permutation gel electrophoresis assay. Individual acetylated species of core histones from butyrate treated HeLa cells were isolated and reconstituted into nucleosomes using a 5S rDNA nucleosome positioning DNA sequence from sea urchin. These nucleosomes were characterized by sulfhydryl group probing, nucleoprotein particle gel electrophoresis and DNase I footprinting. Fully acetylated species of histones H3 and H4 were also reconstituted in closed circular minichromosomes and the effect of DNA topology changes caused by acetylation was studied. Finally, protamines isolated from human sperm were characterized and a full set of core histones were isolated and characterized. 7 refs.

• Research Organization: California Univ., Davis, CA (United States)
• Sponsoring Organization: DOE; USDOE, Washington, DC (United States)
• DOE Contract Number: FG03-88ER60673
• OSTI ID: 6000035
• Report Number(s): DOE/ER/60673-T2; ON: DE92003772
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ACETYLATION
ACYLATION
CHEMICAL REACTIONS
CHROMATIN
COAGULANTS
COHERENT SCATTERING
DICHROISM
DIFFRACTION
DOCUMENT TYPES
DRUGS
ELECTROPHORESIS
HEMATOLOGIC AGENTS
HEPARIN ANTAGONISTS
HISTONES
NEUTRON DIFFRACTION
NUCLEOPROTEINS
NUCLEOSOMES
ORGANIC COMPOUNDS
PROGRESS REPORT
PROTAMINES
PROTEINS
SCATTERING
SMALL ANGLE SCATTERING
X-RAY DIFFRACTION