Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin.
The high mobility group proteins 1 and 2 (HMG1/2) and histone B4 are major components of chromatin within the nuclei assembled during the incubation of Xenopus sperm chromatin in Xenopus egg extract. To investigate their potential structural and functional roles, we have cloned and expressed Xenopus HMG1 and histone B4. Purified histone B4 and HMG1 form stable complexes with nucleosomes including Xenopus 5S DNA. Both proteins associate with linker DNA and stabilize it against digestion with micrococcal nuclease, in a similar manner to histone H1. However, neither histone B4 nor HMG1 influence the DNase I or hydroxyl radical digestion of DNA within the nucleosome core. We suggest that HMG1/2 and histone B4 have a shared structural role in organizing linker DNA in the nucleosome.
Nightingale
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K
Laboratory of Molecular Embryology, National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892-2710, USA.
Dimitrov
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S
Reeves
R
R
Wolffe
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AP
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002843:Chromatin / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D004247:DNA / Q000737:chemistry / Q000235:genetics; D017931:DNA Primers / Q000235:genetics; D005260:Female; D006609:High Mobility Group Proteins / Q000737:chemistry* / Q000235:genetics; D006657:Histones / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D066298:In Vitro Techniques; D008297:Male; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009707:Nucleosomes / Q000737:chemistry / Q000235:genetics; D010063:Ovum / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D013094:Spermatozoa / Q000737:chemistry; D014981:Xenopus
D002843:Chromatin; D017931:DNA Primers; D006609:High Mobility Group Proteins; D006657:Histones; D009707:Nucleosomes; D004247:DNA