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Nuclear transport of H1 histones meets the criteria of a nuclear localization signal—mediated process
Author(s) -
Kurz M.,
Doenecke D.,
Albig W.
Publication year - 1997
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19970315)64:4<573::aid-jcb5>3.0.co;2-o
Subject(s) - nuclear localization sequence , nuclear transport , digitonin , cytoplasm , nls , cell nucleus , histone h1 , histone , wheat germ agglutinin , nucleus , importin , ran , microbiology and biotechnology , chemistry , biology , biochemistry , dna , membrane , lectin
Abstract We have studied the nuclear transport of H1 histones using the digitonin permeabilization assay system in order to establish the transport requirements for H1 translocation to the nucleus. Using HeLa cells and fluorescence‐labeled calf thymus H1, we show that the H1 nuclear transport in permeabilized cells requires the addition of cytoplasmic extract. Furthermore, it can be blocked by energy depletion and by chilling or by addition of wheat germ agglutinin or by nonhydrolyzable GTP analogs. Thus, the import of H1 histones follows the criteria established for nuclear import mediated by nuclear localization signals (NLS). The distribution of basic amino acids in average H1 sequences, however, does not allow the assignment of a specific element as a classical NLS. J. Cell. Biochem. 64:573–578. © 1997 Wiley‐Liss, Inc.