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Mol. Cell. Biol., 10 1997, 5843-5855, Vol 17, No. 10
HF Ding, M Bustin and U Hansen
Histone H1 promotes the generation of a condensed, transcriptionally
inactive, higher-order chromatin structure. Consequently, histone H1
activity must be antagonized in order to convert chromatin to a
transcriptionally competent, more extended structure. Using simian virus 40
minichromosomes as a model system, we now demonstrate that the nonhistone
chromosomal protein HMG-14, which is known to preferentially associate with
active chromatin, completely alleviates histone H1- mediated inhibition of
transcription by RNA polymerase II. HMG-14 also partially disrupts histone
H1-dependent compaction of chromatin. Both the transcriptional enhancement
and chromatin-unfolding activities of HMG-14 are mediated through its
acidic, C-terminal region. Strikingly, transcriptional and structural
activities of HMG-14 are maintained upon replacement of the C-terminal
fragment by acidic regions from either GAL4 or HMG-2. These data support
the model that the acidic C terminus of HMG-14 is involved in unfolding
higher-order chromatin structure to facilitate transcriptional activation
of mammalian genes.
Copyright © 1997, American Society for Microbiology
Alleviation of histone H1-mediated transcriptional repression and chromatin compaction by the acidic activation region in chromosomal protein HMG-14
Dana-Farber Cancer Institute, and Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
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