Effects of HMGN1 on chromatin structure and SWI/SNF-mediated chromatin remodeling
Document Type
Journal ArticlePublication Date
2005-10-29Keywords
Adenosine TriphosphateAnimals
Antibodies
Blotting, Western
Chickens
Chromatin
DNA
Dose-Response Relationship, Drug
Electrophoresis, Polyacrylamide Gel
HMGN1 Protein
Humans
Magnesium Chloride
Nucleosomes
Plasmids
Protein Binding
Protein Structure, Tertiary
Sodium Dodecyl Sulfate
Time Factors
Transcription Factors
Transcription, Genetic
Cell Biology
Life Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
The dynamic modulation of chromatin structure is determined by many factors, including enzymes that modify the core histone proteins, enzymes that remodel the structure of chromatin, and factors that bind to genomic DNA to affect its structure. Previous work indicates that the nucleosome binding family of high mobility group proteins (HMGN) facilitates the formation of a chromatin structure that is more conducive for transcription. SWI/SNF complexes are ATP-dependent chromatin remodeling enzymes that alter nucleosome structure to facilitate the binding of various regulatory proteins to chromatin. Here we examine the structural consequences of reconstituting chromatin with HMGN1 and the resulting effects on hSWI/SNF function. We demonstrate that HMGN1 decreases the sedimentation velocity of nucleosomal arrays in low ionic strength buffers but has little effect on the structure of more highly folded arrays. We further demonstrate that HMGN1 does not affect SWI/SNF-dependent chromatin remodeling on either mononucleosomes or nucleosomal arrays, indicating that SWI/SNF functions independently of HMGN1.Source
J Biol Chem. 2005 Dec 16;280(50):41777-83. Epub 2005 Oct 27. Link to article on publisher's siteDOI
10.1074/jbc.M509637200Permanent Link to this Item
http://hdl.handle.net/20.500.14038/42325PubMed ID
16253989Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1074/jbc.M509637200