1995
DOI: 10.1016/s1067-2389(06)80010-5
|View full text |Cite
|
Sign up to set email alerts
|

[7] Experimental analysis of transcription factor-nucleosome interactions

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
6
0

Year Published

1996
1996
2001
2001

Publication Types

Select...
5
1

Relationship

0
6

Authors

Journals

citations
Cited by 6 publications
(6 citation statements)
references
References 32 publications
0
6
0
Order By: Relevance
“…Acetylation occurs at lysine residues on the N-terminal tails of histones, resulting in alterations in shown in Figure 4. Seven surgical samples, four from adjacent normal tissues (lanes 1-4 in Figure 4) and three from colorectal nucleosomal conformation, thus increasing the accessibility of transcription regulatory proteins to chromatin templates (28). carcinoma tissues (lanes 5-7 in Figure 4), from patients with colon carcinoma were examined.…”
Section: A Possible Relationship Between Histone Acetylation Regulatmentioning
confidence: 99%
“…Acetylation occurs at lysine residues on the N-terminal tails of histones, resulting in alterations in shown in Figure 4. Seven surgical samples, four from adjacent normal tissues (lanes 1-4 in Figure 4) and three from colorectal nucleosomal conformation, thus increasing the accessibility of transcription regulatory proteins to chromatin templates (28). carcinoma tissues (lanes 5-7 in Figure 4), from patients with colon carcinoma were examined.…”
Section: A Possible Relationship Between Histone Acetylation Regulatmentioning
confidence: 99%
“…The reaction was most efficient in the presence of multiple GAGA boxes spread over a distance of 150 bp, and suffered from progressive deletion of binding sites. This situation is reminiscent of the above-mentioned model reactions, which demonstrated that binding of GAL4-AH to multiple sites in a nucleosome can initiate at the loosely associated DNA at nucleosome edges and proceed cooperatively until even sequences close to the dyad axis of the particle are invaded (34). Spread-out GAGA boxes over a considerable area ensure that there will always be a binding site in the linker, even when nucleosomes are assembled with no preferred position.…”
Section: Chromatin Remodeling By Gaga Factor Requires Atp Hydrolysismentioning
confidence: 96%
“…The acetylation of H4 facilitates binding of be the natural substrate for such an activity. The Drosophila homolog of Snf2, Brahma, is present in a complex that fractionates Gal4 to nucleosomal DNA [85], and acetylation of the core histones enhances transcription by RNA polymerase III from a separately from NURF. This result may be consistent with the vast differences in the apparent size and complexity of the nucleosomal template [86].…”
Section: Chromatin-remodelling Machinesmentioning
confidence: 99%
“…The use of in vitro experiments has demonstrated H4 enhances the activation of the MMTV promoter by one or other transactivator but inhibits the synergism between these that the tryptic removal of the N-termini of the core histones results in increased binding of a classical transactivator, Gal4-two [49]. In addition to this nucleosome-dependent synergism the problem of nucleosomal repression at this promoter may be AH, to a nucleosomal binding site, implicating the nucleosome in the control of activated transcription [40].…”
mentioning
confidence: 99%