The ability of PARP1 to control cellular processes is regulated
by nucleosomes — the basic unit of DNA packaging, consisting of a segment of DNA wound in sequence around eight histone protein cores, similar to a thread wrapped around a spool.
Li M, Hada A, Sen P, Olufemi L, Hall MA, Smith BY, Forth S, McKnight JN, Patel A, Bowman GD, Bartholomew B, Wang MD. (2015) Dynamic regulation of transcription factors
by nucleosome remodeling.
Not exact matches
«Our paper shows that suppressing ASF1 induces ALT
by affecting
nucleosome assembly,» he says.
Genomic DNA is packaged into
nucleosomes, which are formed
by histone proteins that have DNA wrapped around them.
Our genes are packaged into cells
by wrapping them around protein structures called
nucleosomes.
Made up of
nucleosomes — roll - shaped bundles of DNA and protein — the heterochromatin is connected
by a velcro - like feature called «Heterochromatin Protein 1 (HP1).»
In the new study, Tulin and his colleagues reevaluated how PARP1 is activated
by changes in the
nucleosome.
Since many of the genes containing «fragile»
nucleosomes are controlled in a continuous manner
by nutrient availability, modulation of promoter
nucleosome stability may be a strategy used to coordinate growth - related transcription on a genome - wide level.
When a given gene needs to be transcribed to create new proteins, its promoter region must be unwrapped from the
nucleosome so that it can be accessed
by the factors involved in initiating the transcription process.
One type, characterized
by the presence of dynamic, unstable,
nucleosomes, is found at highly expressed genes, such as those involved in the control of cell growth and division.
«We have revealed the existence of two types of promoters, which differ
by the presence of «fragile»
nucleosomes,» says Slawomir Kubik, first author of the study and researcher at UNIGE.
Human cytomegalovirus major immediate early 1 protein targets host chromosomes
by docking to the acidic pocket on the
nucleosome surface.
The forward - and reverse - oriented peaks were usually separated
by around 180 base pairs, and corresponded to
nucleosome boundaries.
The evidence for this comes from observing 30 nm and 120 nm wide fibres formed
by DNA and
nucleosomes purified from cells.
BAZ2A is an essential component of the nucleolar remodeling complex (NoRC), which mediates recruitment of histone modifyine enzymes and DNA methylase involved in the silencing of ribosomal RNA transcription
by RNA polymerase I. BAZ2B is believed to be involved in regulating
nucleosome mobilization along linear DNA.
After DNA replication,
nucleosome density is maintained
by incorporating newly synthesized histones besides the recycling of parental histones (Figure 1).