World Library  
Flag as Inappropriate
Email this Article

Histone-modifying enzymes

Article Id: WHEBN0012139474
Reproduction Date:

Title: Histone-modifying enzymes  
Author: World Heritage Encyclopedia
Language: English
Subject: GC box, KMT2A, Response element, PRMT4 pathway, Intrinsic termination
Collection: Epigenetics, Genetics, Proteins
Publisher: World Heritage Encyclopedia

Histone-modifying enzymes

Histone-Modifying Enzymes, the sites for modification are marked in color.

The packaging of the eukaryotic genome into highly condensed chromatin makes it inaccessible to the factors required for gene transcription, DNA replication, recombination and repair. Eukaryotes have developed intricate mechanisms to overcome this repressive barrier imposed by the chromatin. The nucleosome is composed of an octamer of the four core histones (H3, H4, H2A, H2B) around which 147 base pairs of DNA are wrapped. Several distinct classes of enzyme can modify histones at multiple sites.[1] The figure on the right enlists those histone-modifying enzymes whose specificity has been determined. There are at least eight distinct types of modifications found on histones (see the legend box on the top left of the figure). Enzymes have been identified for acetylation,[2] methylation,[3] demethylation,[4] phosphorylation,[5] ubiquitination,[6] sumoylation,[7] ADP-ribosylation,[8] deimination,[9][10] and proline isomerization.[11] For a detailed example of histone modifications in transcription regulation see RNA polymerase control by chromatin structure and table Influence of modifications on gene expression in mammalian cells.

See also


  1. ^
  2. ^
  3. ^
  4. ^
  5. ^
  6. ^
  7. ^
  8. ^
  9. ^
  10. ^
  11. ^
This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.

Copyright © World Library Foundation. All rights reserved. eBooks from Hawaii eBook Library are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.