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Distinct importin recognition properties of histones and chromatin assembly factors
Author(s) -
Johnson-Saliba Melanie,
Siddon Nicole A,
Clarkson Michael J,
Tremethick David J,
Jans David A
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01142-x
Subject(s) - importin , chromatin , nuclear transport , histone , acetylation , microbiology and biotechnology , cytoplasm , nls , histone h1 , nuclear localization sequence , histone code , nuclear protein , biology , cell nucleus , nucleosome , chemistry , biochemistry , gene , transcription factor
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.