Faculty Collaboration Database

The Heterochromatin Protein 1 family. Genome Biol 2006;7(7):228

Date

01/17/2007

Pubmed ID

17224041

Pubmed Central ID

PMC1779566

DOI

10.1186/gb-2006-7-7-228

Scopus ID

2-s2.0-33845192953 (requires institutional sign-in at Scopus site)   205 Citations

Abstract

Heterochromatin Protein 1 (HP1) was first discovered in Drosophila as a dominant suppressor of position-effect variegation and a major component of heterochromatin. The HP1 family is evolutionarily conserved, with members in fungi, plants and animals but not prokaryotes, and there are multiple members within the same species. The amino-terminal chromodomain binds methylated lysine 9 of histone H3, causing transcriptional repression. The highly conserved carboxy-terminal chromoshadow domain enables dimerization and also serves as a docking site for proteins involved in a wide variety of nuclear functions, from transcription to nuclear architecture. In addition to heterochromatin packaging, it is becoming increasingly clear that HP1 proteins have diverse roles in the nucleus, including the regulation of euchromatic genes. HP1 proteins are amenable to posttranslational modifications that probably regulate these distinct functions, thereby creating a subcode within the context of the 'histone code' of histone posttranslational modifications.

Author List

Lomberk G, Wallrath L, Urrutia R

Authors

Gwen Lomberk PhD Professor in the Surgery department at Medical College of Wisconsin
Raul A. Urrutia MD Center Director, Professor in the Surgery department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Animals
Chromosomal Proteins, Non-Histone
Drosophila
Evolution, Molecular
Humans
Phylogeny
Protein Processing, Post-Translational