Localization of DNA methyltransferase in the chromatin of Friend erythroleukemia cells.
AUTOR(ES)
Creusot, F
RESUMO
Chromatin fragments released from intact Friend erythroleukemia cell nuclei during limited incubation with micrococcal nuclease, DNase II or DNase I were analyzed to determine the distribution of DNA methyltransferase in chromatin. The enzyme was released in a free form when internucleosomal DNA was digested with micrococcal nuclease but was found associated with Mg++-precipitable polynucleosomes after DNase II digestion. Less than 25% of the enzyme was released from nuclei incubated with DNase I under conditions where transcriptionally active chromatin should have been completely digested. These results indicated that the bulk of DNA methyltransferase was bound to "linker" DNA in condensed regions of chromatin. Preferential rebinding of free enzyme to linker DNA was also demonstrated in vitro. The possibility that chromatin proteins play a role in regulating access of DNA methyltransferase to specific sites in DNA is discussed in light of these findings.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=327525Documentos Relacionados
- Subcellular localization of the env-related glycoproteins in Friend erythroleukemia cells.
- Growth-dependent expression of multiple species of DNA methyltransferase in murine erythroleukemia cells.
- Detection of glucocorticoid receptors on Friend erythroleukemia cells.
- Nucleosome-associated proteins and phosphoproteins of differentiating Friend erythroleukemia cells.
- Role of the PU.1 transcription factor in controlling differentiation of Friend erythroleukemia cells.
