Distinct importin recognition properties of histones and chromatin assembly factors.
Date
2000
Authors
Johnson-Saliba, Melanie
Siddon, Nicole
Clarkson, M J
Tremethick, David
Jans, David A
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier
Abstract
Synthesis of the protein components of nuclear chromatin occurs in the cytoplasm, necessitating specific import into the nucleus. Here, we report the binding affinities of the nuclear localisation sequence (NLS)-binding importin subunits for a range of histones and chromatin assembly factors. The results suggest that import of histones to the nucleus may be mediated predominantly by importin β1, whereas the import of the other components probably relies on the conventional α/β1 import pathway. Differences in recognition by importin β1 were observed between histone H2A and the variant H2AZ, as well as between histone H3/4 with or without acetylation. The results imply that different histone variants may possess distinct nuclear import properties, with acetylation possibly playing an inhibitory role through NLS masking.
Description
Keywords
Keywords: chromatin associated protein; histone; histone H2A; karyopherin; unclassified drug; article; binding affinity; chromatin; controlled study; mouse; nonhuman; nucleosome; priority journal; protein localization; protein transport; Xenopus; Acetylation; Amino Chromatin-associated protein; Histone; Histone acetylation; Histone variant; Importin; NAP-1
Citation
Collections
Source
FEBS Letters
Type
Journal article
Book Title
Entity type
Access Statement
License Rights
Restricted until
2037-12-31