Document Detail

Perceiving the epigenetic landscape through histone readers.
MedLine Citation:
PMID:  23211769     Owner:  NLM     Status:  MEDLINE    
Post-translational modifications (PTMs) of histones provide a fine-tuned mechanism for regulating chromatin structure and dynamics. PTMs can alter direct interactions between histones and DNA and serve as docking sites for protein effectors, or readers, of these PTMs. Binding of the readers recruits or stabilizes various components of the nuclear signaling machinery at specific genomic sites, mediating fundamental DNA-templated processes, including gene transcription and DNA recombination, replication and repair. In this review, we highlight the latest advances in characterizing histone-binding mechanisms and identifying new epigenetic readers and summarize the functional significance of PTM recognition.
Catherine A Musselman; Marie-Eve Lalonde; Jacques Côté; Tatiana G Kutateladze
Related Documents :
22155599 - Novel cationic liposomes provide highly efficient delivery of dna and rna into dendriti...
2406589 - Induction of error-free dna repair in escherichia coli by thiamine deprivation.
23565679 - Measuring and modeling the kinetics of individual dna-dna polymerase complexes on a nan...
23471669 - Two distinct thermal stabilities of dna and enzymatic activities of dnase i in a mult...
18379129 - Genetic analysis of the neurospora crassa rad14 homolog mus-43 and the rad10 homolog mu...
20816939 - Investigation of riboflavin sensitized degradation of purine and pyrimidine derivatives...
9042949 - Use of phage display for isolation and characterization of single-chain variable fragme...
22095249 - Laboratory exposure of oreochromis niloticus to crude microcystins (containing microcys...
213439 - Two epstein-barr virus-associated dna polymerase activities.
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Nature structural & molecular biology     Volume:  19     ISSN:  1545-9985     ISO Abbreviation:  Nat. Struct. Mol. Biol.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-12-05     Completed Date:  2013-02-04     Revised Date:  2014-03-19    
Medline Journal Info:
Nlm Unique ID:  101186374     Medline TA:  Nat Struct Mol Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1218-27     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
DNA / chemistry,  genetics
DNA Methylation
DNA Repair
DNA Replication
Epigenesis, Genetic*
Histones / chemistry*
Models, Molecular
Recombination, Genetic
Transcription, Genetic
Grant Support
64289-3//Canadian Institutes of Health Research; 87253-1//Canadian Institutes of Health Research; CA113472/CA/NCI NIH HHS; F32 HL096399/HL/NHLBI NIH HHS; GM096863/GM/NIGMS NIH HHS; MOP-14308//Canadian Institutes of Health Research; MOP-64289//Canadian Institutes of Health Research; R01 CA113472/CA/NCI NIH HHS; R01 GM096863/GM/NIGMS NIH HHS
Reg. No./Substance:
0/Histones; 9007-49-2/DNA

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

Previous Document:  Antibacterial activity of probiotic candidates for oral health.
Next Document:  Effect of Age on Treatment, Trends and Outcome of Patients Hospitalized With Atrial Fibrillation: In...