Format:
Online-Ressource
ISSN:
1460-2075
Content:
The heterochromatin protein 1 (HP1) family of proteins is involved in gene silencing via the formation of heterochromatic structures. They are composed of two related domains: an N‐terminal chromo domain and a C‐terminal shadow chromo domain. Present results suggest that chromo domains may function as protein interaction motifs, bringing together different proteins in multi‐protein complexes and locating them in heterochromatin. We have previously determined the structure of the chromo domain from the mouse HP1β protein, MOD1. We show here that, in contrast to the chromo domain, the shadow chromo domain is a homodimer. The intact HP1β protein is also dimeric, where the interaction is mediated by the shadow chromo domain, with the chromo domains moving independently of each other at the end of flexible linkers. Mapping studies, with fragments of the CAF1 and TIF1β proteins, show that an intact, dimeric, shadow chromo domain structure is required for complex formation.
In:
volume:19
In:
number:7
In:
year:2000
In:
pages:1587-1597
In:
extent:11
In:
European Molecular Biology Organization, The EMBO journal, Heidelberg : EMBO Press, 1982-, 19, Heft 7 (2000), 1587-1597 (gesamt 11), 1460-2075
Language:
English
DOI:
10.1093/emboj/19.7.1587
URN:
urn:nbn:de:101:1-2023110104290589871675
URL:
https://doi.org/10.1093/emboj/19.7.1587
URL:
https://nbn-resolving.org/urn:nbn:de:101:1-2023110104290589871675
URL:
https://d-nb.info/1308125887/34
URL:
https://doi.org/10.1093/emboj/19.7.1587
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