Alternative nucleosomal structure

AccessScience ◽  
2015 ◽  
Keyword(s):  
Nucleosomal Structure

scholarly journals Variant Chromatin Structure of theoriP Region of Epstein-Barr Virus and Regulation of EBER1 Expression by Upstream Sequences andoriP

2001 ◽  
Vol 75 (13) ◽  
pp. 6235-6241 ◽  
Author(s):  
Barbara Wensing ◽  
Albert Stühler ◽  
Peter Jenkins ◽  
Martine Hollyoake ◽  
Claudio Elgueta Karstegl ◽  
...  
Keyword(s):  
Epstein Barr Virus ◽  
Virus Genome ◽  
Micrococcal Nuclease ◽  
Matrix Attachment Region ◽  
Barr Virus ◽  
Latently Infected ◽  
Attachment Region ◽  
Nuclear Matrix Attachment Region ◽  
Epstein Barr ◽  
Nucleosomal Structure

ABSTRACT Most of the Epstein-Barr virus genome in latently infected cells is in a standard nucleosomal structure, but the region encompassingoriP and the Epstein-Barr virus-encoded small RNA (EBER) genes shows a distinctive pattern when digested with micrococcal nuclease. This pattern corresponds to a previously mapped nuclear matrix attachment region. Although the EBER genes are adjacent to oriP, there is only a two- to fourfold effect oforiP on EBER expression. However, sequences containing a consensus ATF site upstream of EBER1 are important for EBER1 expression.

scholarly journals A DNA fragment containing the upstream activator sequence determines nucleosome positioning of the transcriptionally repressed PHO5 gene of Saccharomyces cerevisiae.

1986 ◽  
Vol 6 (7) ◽  
pp. 2298-2304 ◽  
Author(s):  
L W Bergman
Keyword(s):  
Transcriptional Regulation ◽  
Nucleosome Positioning ◽  
Vector System ◽  
Growth Media ◽  
Flanking Sequences ◽  
Dna Fragment ◽  
Acid Phosphatase Gene ◽  
Nucleosomal Structure ◽  
Relationship Of ◽  
Pho5 Gene

The functional relationship of nucleosome positioning and gene expression is not known. Using high-copy plasmids, containing the yeast phosphate-repressible acid phosphatase gene (PHO5) and the TRP1/ARS1 vector system, I have determined the nucleosomal structure of the 5' region of the PHO5 gene and demonstrated that the nucleosomal positioning of this region is independent of orientation or position in the various plasmid constructions utilized. However, deletion of a 278-base pair BamHI-ClaI fragment from the 5'-flanking sequences of the PHO5 gene causes the nucleosome positioning to become dependent on orientation or position in the plasmids tested. Use of PHO5-CYC1-lACZ fusions have demonstrated that this DNA fragment contains the sequences responsible for the transcriptional regulation of the PHO5 gene in response to the level of phosphate in the growth media. The nucleosome positioning in the 5' region of PHO5 may be determined by an interaction with the sequences or machinery responsible for transcriptional regulation of the gene.

scholarly journals Nucleosomal structure at hyperacetylated loci probed in nuclei by DNA-histone crosslinking

1993 ◽  
Vol 21 (20) ◽  
pp. 4734-4738 ◽  
Author(s):  
Konstantin K. Ebralidse ◽  
Tim R. Hebbes ◽  
Alison L. Clayton ◽  
Alan W. Thorne ◽  
Colyn Crane-Robinson
Keyword(s):  
Nucleosomal Structure

Nucleosomal structure as probed by H3 histone thiol reactivity

1987 ◽  
Vol 10 (1) ◽  
pp. 1-13 ◽  
Author(s):  
Nicoletta Ferrari ◽  
Ulrich Pfeffer ◽  
Giorgio Vidali
Keyword(s):  
Thiol Reactivity ◽  
Nucleosomal Structure

scholarly journals Use of RNA polymerase as an enzymatic probe of nucleosomal structure

1980 ◽  
Vol 8 (17) ◽  
pp. 3851-3864 ◽  
Author(s):  
Henry G. Hodo ◽  
Chintaman G. Sahasrabuddhe ◽  
Mary F. Plishker ◽  
Grady F. Saunders
Keyword(s):  
Rna Polymerase ◽  
Nucleosomal Structure

scholarly journals Nucleosomal structure of SV40 minichromosome as revealed by micrococcal nuclease action

FEBS Letters ◽  
1981 ◽  
Vol 125 (1) ◽  
pp. 35-38 ◽  
Author(s):  
Sergei Nedospasov ◽  
Alexander Shakhov ◽  
Georgii Georgiev
Keyword(s):  
Micrococcal Nuclease ◽  
Nucleosomal Structure

scholarly journals Interaction between second generation anthracyclines and DNA in the nucleosomal structure

1991 ◽  
Vol 19 (9) ◽  
pp. 2309-2314 ◽  
Author(s):  
C. Cera ◽  
G. Palù ◽  
S.Marciani Magno ◽  
M. Palumbo
Keyword(s):  
Second Generation ◽  
Nucleosomal Structure

scholarly journals Histone Deacetylase Inhibitors in the Treatment of Hematological Malignancies and Solid Tumors

2011 ◽  
Vol 2011 ◽  
pp. 1-12 ◽  
Author(s):  
Mario Federico ◽  
Luigi Bagella
Keyword(s):  
Solid Tumors ◽  
Histone Deacetylases ◽  
Histone Deacetylase Inhibitors ◽  
Hematological Malignancies ◽  
Histone Proteins ◽  
Histone Deacetylases Inhibitors ◽  
Recent Developments ◽  
Nucleosomal Structure

The human genome is epigenetically organized through a series of modifications to the histone proteins that interact with the DNA. In cancer, many of the proteins that regulate these modifications can be altered in both function and expression. One example of this is the family of histone deacetylases (HDACs), which as their name implies remove acetyl groups from the histone proteins, allowing for more condensed nucleosomal structure. HDACs have increased expression in cancer and are also believed to promote carcinogenesis through the acetylation and interaction with key transcriptional regulators. Given this, small molecule histone deacetylases inhibitors have been identified and developed, which not only inhibit HDACs, but can also lead to growth arrest, differentiation, and/or apoptosis in tumors bothin vitroandin vivo. Here, we will discuss some of the recent developments in clinical trials utilizing HDACs inhibitors for the treatment of both hematological malignancies as well as solid tumors.

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