The globular domain of histone H1 is sufficient to direct specific gene repression in early Xenopus embryos

Danielle Vermaak, Oliver C. Steinbach, Stephan Dimitrov, Ralph A.W. Rupp, Alan P. Wolffe

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49 Citations (Scopus)


One molecule of a linker histone such as histone H1 is incorporated into every metazoan nucleosome [1]. Histone H1 has three distinct structural domains: the positively charged amino-terminal and carboxy-terminal tails are separated by a globular domain that is similar to the winged-helix motif found in sequence-specific DNA-binding proteins [2]. The globular domain interacts with DNA immediately contiguous to that wrapped around the core histones [3,4], whereas the tail domains are important for the compaction of nucleosomal arrays [5]. Experiments in vivo indicate that histone H1 does not function as a global transcriptional repressor, but instead has more specific regulatory roles [6-9]. In Xenopus, maternal stores of the B4 linker histone that are assembled into chromatin during the early cleavage divisions are replaced by somatic histone H1 during gastrulation [10]. This transition in chromatin composition causes the repression of genes encoding oocyte-type 5S rRNAs, and restricts the competence of ectodermal cells to differentiate into mesoderm [6,9-11]. Here, we demonstrate that the globular domain of histone H1 is sufficient for directing gene-specific transcriptional repression and for restricting the mesodermal competence of embryonic ectoderm. We discuss our results in the context of specific structural roles for this domain in the nucleosome.

Original languageEnglish
Pages (from-to)533-536
Number of pages4
JournalCurrent Biology
Issue number9
Publication statusPublished - 23 Apr 1998


ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

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