Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Patterns of histone acetylation.

A W Thorne1, D Kmiciek, K Mitchelson

  • 1Biophysics Laboratories, Portsmouth Polytechnic, England.

European Journal of Biochemistry
|November 13, 1990
PubMed
Summary

Histone acetylation site specificity was investigated in pig and HeLa cells. Results show distinct patterns for histones H3, H4, and H2B, indicating specific functional roles beyond generalized charge reduction.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Forces for Folding.

Acta naturae·2021
Same author

Thermodynamic basis of the α-helix and DNA duplex.

European biophysics journal : EBJ·2021
Same author

Linker histones: History and current perspectives.

Biochimica et biophysica acta·2015
Same author

MicroRNA-133b is a key promoter of cervical carcinoma development through the activation of the ERK and AKT1 pathways.

Oncogene·2011
Same author

Rapid, accurate determination of multidrug resistance in M. tuberculosis isolates and sputum using a biochip system.

The international journal of tuberculosis and lung disease : the official journal of the International Union against Tuberculosis and Lung Disease·2009
Same author

Regulation of myofibroblast transdifferentiation by DNA methylation and MeCP2: implications for wound healing and fibrogenesis.

Cell death and differentiation·2006

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • Core histones (H3, H4, H2B, H2A) undergo reversible lysine acetylation.
  • Histone acetylation is linked to transcription, DNA replication, and spermatogenesis.
  • Understanding site-specific acetylation is crucial for elucidating its diverse functions.

Purpose of the Study:

  • To investigate the specificity of lysine residue acetylation in histones H3, H4, and H2B.
  • To compare acetylation patterns in pig thymus and HeLa cells, with and without butyrate treatment.
  • To determine if histone acetylation specificity is maintained under conditions that increase modification levels.

Main Methods:

  • Histone extraction from pig thymus and HeLa cells.
  • Analysis of mono-, di-, and triacetylated forms of histones H3, H4, and H2B.

Related Experiment Videos

  • Comparison of acetylation site utilization across different histone types and cell treatments.

    • Main Results:

    • Histone H3 exhibits strict acetylation order: Lys14, then Lys23, then Lys18.
    • Histone H4 monoacetylation occurs at Lys16, with further acetylation progressing N-terminally.
    • Histone H2B shows lower site specificity, preferring Lys12 and Lys15.

    Conclusions:

    • Lysine acetylation of core histones is a highly specific process.
    • Site specificity suggests distinct functional roles for different acetylation patterns.
    • Acetylation's effects are unlikely due to generalized charge reduction in histone N-terminal domains.