Control of RNA synthesis by chromatin proteins.
AUTOR(ES)
Cedar, H
RESUMO
The effect of chromatin proteins on template activity has been studied. Using both E. coli RNA polymerase and calf thymmus polymerase B we have measured the number of initiation sites on chromatin and various histone-DNA complexes. Chromatin can be reconstituted with histone proteins alone and this complex is still a restricted template for RNA synthesis. The removal of histone f1 causes a large increase in the template activity. Chromatin is then treated with Micrococcal nuclease and the DNA fragments protected from nuclease attack ("covered DNA") are isolated. Alternatively, the chromatin is titrated with poly-D-lysine, and by successive treatment with Pronase and nuclease, the DNA regions accessible to polylysine are isolated ("open DNA"). Both fractions were tested for template activity. It was found that RNA polymerase initiation sites are distributed equally in open and covered region DNA.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=343026Documentos Relacionados
- Stimulation of vesicular stomatitis virus in vitro RNA synthesis by microtubule-associated proteins.
- Regulation of mitochondrial protein synthesis by cytoplasmic proteins.
- DNA unwinding component of the nonhistone chromatin proteins.
- Asynchronous synthesis of erythrocyte membrane proteins.
- Polyoma virus minichromosomes: poly ADP-ribosylation of associated chromatin proteins.