Santoro R, D'Erme M, Reale A, Strom R, Caiafa P
Department of Biochemical Sciences, University of Rome La Sapienza, Italy.
Biochem Biophys Res Commun. 1993 Jan 15;190(1):86-91. doi: 10.1006/bbrc.1993.1014.
The loosely and tightly bound H1 histone isoforms were shown to exert, on the in vitro methylation of linker DNA in H1-depleted oligonucleosomes, inhibitory or activating effects respectively similar to those previously shown in the methylation of Micrococcus luteus dsDNA. When assayed on the enzymic methylation of Micrococcus luteus ssDNA, addition of the tightly bound one resulted in a stimulation similar to that exerted on double-stranded bacterial DNA or on linker DNA from mammalian chromatin, while the loosely bound isoform had no effect whatsoever. The transformation of the "typical" loosely bound H1 isoform into its tightly bound counterpart can be visualized as being an essential event in the modulation of DNA methylation process in eukaryotic chromatin.
