Core nucleosomes by digestion of reconstructed histone-DNA complexes
نویسندگان
چکیده
منابع مشابه
Core nucleosomes by digestion of reconstructed histone-DNA complexes.
Reconstructed complexes of the inner histones (H2A, H2B, H3, H4) and a variety of DNAs were digested with micrococcal nuclease to yield very homogeneous populations of core nucleosomes (nu 1). Nucleosomes containing Micrococcus luteus DNA (72% G+C); chicken DNA (43% G+C), Clostridium perfringens DNA (29% G+C); or poly(A-dT.poly(dA-dT) have been examined by circular dichroism, thermaldetenatura...
متن کاملBINDING OF THE ANTITUMOR DRUG ADRIAMYCIN TO DNA-HISTONE COMPLEXES
Isotherms of the binding of the anthracycIine antibiotic, adriamycin (adriblastin), to DNA histone complexes was studied by means of spectroscopic analysis. The results indicated that: (a) binding of adriamycin to histones reduced the interaction of histones with DNA, (b) binding of the drug to DNA did not change the binding affinity of histone to DNA and, (c) in the explored binding range...
متن کاملHistone Acetyltransferase Complexes Stabilize SWI/SNF Binding to Promoter Nucleosomes
To investigate the function of SWI/SNF in site-specific chromatin remodeling at promoters, we have used a purified system to analyze its distribution, function, and retention following recruitment by a sequence-specific transcription activator. Activator recruitment of SWI/SNF bound the complex to promoter proximal nucleosomes and led to localized nucleosome disruption. However, retention of SW...
متن کاملbinding of the antitumor drug adriamycin to dna-histone complexes
isotherms of the binding of the anthracyciine antibiotic, adriamycin (adriblastin), to dna histone complexes was studied by means of spectroscopic analysis. the results indicated that: (a) binding of adriamycin to histones reduced the interaction of histones with dna, (b) binding of the drug to dna did not change the binding affinity of histone to dna and, (c) in the explored binding range of r
متن کاملStructural aspects of histone complexes and nucleosomes revealed by the accessibility of cysteine side chains.
Chemical modification with 5,5'-dithiobis-(2-nitrobenzoic acid) shows that histone H3 cysteines 110 (chicken) or 96 and 110 (calf) are completely protected in native chromatin and core particles but become unmasked simultaneously during a salt induced dissociation. In whole histone extracted from chicken erythrocyte chromatin, H3 Cys-110 residues experience a uniform environment at 2 M NaCl and...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 1979
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/6.4.1449