Preferential binding of H1e histone to GC-rich DNA

We have investigated the binding of a pure H1 histone, the mouse variant H1e, to a 214 bp fragment of DNA from pBR322. Binding was monitored by observing the effects of the protein on melting of the DNA and by a gel-mobility-shift assay. We found, using this highly purified system, that H1e protein...

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Bibliographic Details
Published in:Biochemistry (Easton) 1994-01, Vol.33 (1), p.384-388
Main Authors: Wellman, Susan E, Sittman, Donald B, Chaires, Jonathan B
Format: Article
Language:English
Subjects:
3T3 Cells
Amino Acid Sequence
Animals
Base Composition
Biological and medical sciences
Chromatin. Chromosome
Circular Dichroism
Conserved Sequence
Cytosine
DNA - chemistry
DNA - metabolism
Fundamental and applied biological sciences. Psychology
Guanine
Histones - chemistry
Histones - metabolism
Leukemia, Erythroblastic, Acute
Mice
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Nucleic Acid Denaturation
Peptide Fragments - chemical synthesis
Peptide Fragments - chemistry
Peptide Fragments - metabolism
Protein Conformation
Protein Denaturation
Tumor Cells, Cultured
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Summary:We have investigated the binding of a pure H1 histone, the mouse variant H1e, to a 214 bp fragment of DNA from pBR322. Binding was monitored by observing the effects of the protein on melting of the DNA and by a gel-mobility-shift assay. We found, using this highly purified system, that H1e protein binds preferentially and cooperatively to the GC-rich region of the DNA. A chemically synthesized peptide containing 25 residues, corresponding to a region of the carboxyl-terminal domain of H1e, shows the same sequence preference but does not exhibit cooperativity.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00167a049