Document Detail

Molecular Dynamics Simulations Demonstrate the Regulation of DNA-DNA Attraction by H4 Histone Tail Acetylations and Mutations.
MedLine Citation:
PMID:  24740714     Owner:  NLM     Status:  Publisher    
The positively charged N-terminal histone tails, play a crucial role in chromatin compaction, and are important modulators of DNA transcription, recombination and repair. The detailed mechanism of the interaction of histone tails with DNA remains elusive. To model the unspecific interaction of histone tails with DNA, all-atom molecular dynamics (MD) simulations were carried out for systems of four DNA 22-mers in the presence of 20 or 16 short fragments of the H4 histone tail (variations of the 16-23 a. a. KRHRKVLR sequence, as well as the unmodified fragment a. a.13-20, GGAKRHRK). This setup with high DNA concentration, explicit presence of DNA-DNA contacts, presence of unstructured cationic peptides (histone tails, and K(+) , mimics the conditions of eukaryotic chromatin. A detailed account of the DNA interactions with the histone tail fragments, K(+) and water is presented. Furthermore, DNA structure and dynamics and its interplay with the histone tail fragments binding are analysed. The charged side chains of the lysines and arginines play major roles in the tail-mediated DNA-DNA attraction by forming bridges and by coordinating to the phosphate groups and to the electronegative sites in the minor groove. Binding of all species to DNA is dynamic. The structure of the unmodified fully-charged H4 16-23 a.a. fragment KRHRKVLR is dominated by a stretched conformation. The H4 tail a. a. fragment GGAKRHRK as well as the H4 Lys16 acetylated fragment are highly flexible. The present work allows capturing typical features of the histone tail-counterion-DNA structure, interaction and dynamics.
Nikolay Korolev; Hang Yu; Alexander P Lyubartsev; Lars Nordenskiöld
Related Documents :
11876794 - In situ polymerase chain reaction detection of transfusion-transmitted virus in liver b...
3229594 - Dna methylation in rat liver by daminozide, 1,1-dimethylhydrazine, and dimethylnitrosam...
3101694 - Digestion of repair sites in rat liver dna by endogenous nucleases.
24011044 - Isolation of genomic dna from mammalian cells.
17623884 - Dieldrin elicits a widespread dna repair and antioxidative response in mouse brain.
4184694 - Binding of rabbit gamma globulin by competent bacillus subtilis cultures.
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-4-17
Journal Detail:
Title:  Biopolymers     Volume:  -     ISSN:  0006-3525     ISO Abbreviation:  Biopolymers     Publication Date:  2014 Apr 
Date Detail:
Created Date:  2014-4-17     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372525     Medline TA:  Biopolymers     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2014 Wiley Periodicals, Inc., a Wiley company.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Effect of lowering or restricting sympathectomy levels on compensatory sweating.
Next Document:  Identification of effective Pb resistant bacteria isolated from Lens culinaris growing in lead conta...