Histone H1 subtypes differentially modulate chromatin condensation without preventing ATP-dependent remodeling by SWI/SNF or NURF.
Although ubiquitously present in chromatin, the function of the linker histone subtypes is partly unknown and contradictory studies on their properties have been published. To explore whether the various H1 subtypes have a differential role in the organization and dynamics of chromatin we have incorporated all of the somatic human H1 subtypes into minichromosomes and compared their influence on nucleosome spacing, chromatin compaction and ATP-dependent remodeling. H1 subtypes exhibit different affinities for chromatin and different abilities to promote chromatin condensation, as studied with the Atomic Force Microscope. According to this criterion, H1 subtypes can be classified as weak condensers (H1.1 and H1.2), intermediate condensers (H1.3) and strong condensers (H1.0, H1.4, H1.5 and H1x). The variable C-terminal domain is required for nucleosome spacing by H1.4 and is likely responsible for the chromatin condensation properties of the various subtypes, as shown using chimeras between H1.4 and H1.2. In contrast to previous reports with isolated nucleosomes or linear nucleosomal arrays, linker histones at a ratio of one per nucleosome do not preclude remodeling of minichromosomes by yeast SWI/SNF or Drosophila NURF. We hypothesize that the linker histone subtypes are differential organizers of chromatin, rather than general repressors.
Centre de Regulació Genòmica (CRG), Universitat Pompeu Fabra, Barcelona, Spain.
Jaime
J
Clausell
Nicole
N
Happel
Tracy K
TK
Hale
Detlef
D
Doenecke
Miguel
M
Beato
D000255:Adenosine Triphosphate / Q000737:chemistry*; D000818:Animals; D002843:Chromatin / Q000737:chemistry*; D042002:Chromatin Assembly and Disassembly; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry*; D002875:Chromosomes / Q000378:metabolism; D029721:Drosophila Proteins / Q000737:chemistry*; D004331:Drosophila melanogaster / Q000378:metabolism; D005786:Gene Expression Regulation; D006367:HeLa Cells; D006657:Histones / Q000737:chemistry / Q000235:genetics* / Q000502:physiology*; D006801:Humans; D018625:Microscopy, Atomic Force / Q000379:methods; D009707:Nucleosomes / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D056505:Retinoblastoma-Binding Protein 4 / Q000737:chemistry*; D014157:Transcription Factors / Q000737:chemistry*
C110251:Caf1-55 protein, Drosophila; D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D029721:Drosophila Proteins; D006657:Histones; D009707:Nucleosomes; D056505:Retinoblastoma-Binding Protein 4; C445179:SWI-SNF-B chromatin-remodeling complex; D014157:Transcription Factors; D000255:Adenosine Triphosphate